KR20230054671A - Compositions and methods related to activatable therapeutics - Google Patents

Abstract

Methods, kits, and methods of making and using activatable therapeutics are described herein for assessing the likelihood of a subject responding to activatable therapeutics and compositions. Also described herein are methods for assessing a subject's likelihood of responding to an activatable therapeutic agent. In some cases, the activatable therapeutic agents of the compositions, kits and methods disclosed herein may include sequences from mammalian proteins.

Description

Compositions and methods related to activatable therapeutics

reference statement

This application claims priority from U.S. Provisional Patent Application Serial No. 63/054525, filed July 21, 2020, entitled "COMPOSITIONS AND METHODS RELATED TO ACTIVATABLE THERAPEUTIC AGENTS", which The application is incorporated herein in its entirety.

sequence listing statement

A computer readable form of the sequence listing is submitted with this application by electronic submission and is incorporated herein by reference in its entirety. The sequence listing is contained in a file created on July 15, 2021 with the file name "791-601_20-1831-WO_ST25_FINAL.txt" and is 1700 kb in size.

A key challenge in the development of prodrug therapies is to avoid unwanted immunogenicity and non-specific activation at biological sites in vivo other than the target site. Various release sites have been optimized in vitro and incorporated into prodrugs for programmed and targeted activation, eg, by protease(s) produced naturally in or near diseased tissue(s). Such engineered release segments can form T cell or B cell epitopes that can lead to undesirable immunogenicity in patients. In addition, methods for properly predicting the in vivo response of patients to current prodrugs are lacking. In particular, with respect to protease-activating prodrugs, targeted diseased tissues often contain multiple proteases with varying activities and specificities, which are difficult to reconstitute in vitro and complicate prediction of prodrug activation in vivo. There remains a need to identify new peptide segments that can be included in various prodrug therapeutic, diagnostic and prophylactic compositions for more effective and reliable release mechanisms. There also remains a need to develop more accurate and robust methods for predicting therapeutic response and outcome upon administration of prodrugs or other activatable compositions.

In certain aspects, the present disclosure provides methods for assessing the likelihood that a subject will respond to a therapeutic agent that can be activated by a mammalian protease expressed in the subject, the method comprising:

(a) Determining the presence or amount of in a biological sample from a subject

(i) a polypeptide comprising at least 5, at least 6, at least 7, at least 8, at least 9 or at least 10 contiguous amino acid residues represented in the sequence set forth in column V of Table A (or a subset thereof); or

(ii) a polypeptide comprising at least 5, at least 6, at least 7, at least 8, at least 9 or at least 10 contiguous amino acids shown in the sequence set forth in column IV (or a subset thereof) of Table A ; or

(iii) a polypeptide comprising at least 5, at least 6, at least 7, at least 8, at least 9 or at least 10 contiguous amino acids shown in the sequence set forth in column VI of Table A (or a subset thereof); and

(b) designating the subject as likely to respond to the therapeutic agent if the polypeptide of (i), (ii) or (iii) is present and/or the amount exceeds a threshold value.

In some embodiments of the method for assessing the likelihood of a subject responding to a therapeutic agent, the therapeutic agent comprises a peptide substrate that is susceptible to cleavage by mammalian proteases at cleavable bonds. In some embodiments, the polypeptide of (i), (ii) or (iii) is at least 4, at least 5, at least 6, at least 7 of the peptide substrate that is on the N-terminal or C-terminal side of the cleavable bond. , a portion comprising at least 8, at least 9 or at least 10 contiguous amino acid residues. In some embodiments, the peptide substrate is susceptible to cleavage by a mammalian protease at its cleavable linkage, wherein the polypeptide of (i), (ii) or (iii) is cleaved by the same mammalian protease at its cleavable linkage. is a cleavage product of a reporter polypeptide comprising a substrate sequence susceptible to , wherein the reporter polypeptide comprises the sequence set forth in column II or column III (or a subset thereof) of Table A. In some embodiments, the peptide substrate is susceptible to cleavage by a mammalian protease at the cleavable linkage, wherein the polypeptide of (i), (ii) or (iii) is at least 5% of the peptide substrate comprising the cleavable linkage. It is a cleavage product of a human protein, comprising a portion comprising two or six consecutive amino acid residues.

In some embodiments of the method for assessing the likelihood of a subject responding to a therapeutic agent, the polypeptide of (i) is at least 6, at least 7, at least 8 represented by the sequence set forth in column V of Table A (or a subset thereof). , at least 9 or at least 10 consecutive amino acid residues. In some embodiments, the polypeptide of (ii) comprises at least 6, at least 7, at least 8, at least 9 or at least 10 contiguous amino acids indicated in the sequence set forth in column IV of Table A (or a subset thereof). do. In some embodiments, the polypeptide of (iii) comprises at least 6, at least 7, at least 8, at least 9 or at least 10 contiguous amino acids shown in the sequence set forth in column VI of Table A (or a subset thereof). do.

In some embodiments of a method for assessing the likelihood of a subject responding to a therapeutic agent, (a) comprises determining the presence or amount of any two of (i)-(iii). In some embodiments, (a) includes determining the presence or amount of all three of (i) to (iii).

In some embodiments of a method for assessing the likelihood of a subject responding to a therapeutic agent, the threshold is zero or a nominal threshold. In some embodiments, a biological sample includes a serum or plasma sample. In some embodiments, a biological sample comprises a serum sample. In some embodiments, a biological sample comprises a plasma sample.

In some embodiments of the method for assessing the likelihood of a subject responding to a therapeutic agent, the mammalian protease is a serine protease, cysteine protease, aspartate protease, threonine protease, or metalloproteinase. In some embodiments, the mammalian protease is disintegrin and metalloproteinase domain containing protein 10 (ADAM10), disintegrin and metalloproteinase domain containing protein 12 (ADAM12), disintegrin and metalloproteinase domain containing Protein 15 (ADAM15), Disintegrin and Metalloproteinase Domain Containing Protein 17 (ADAM17), Disintegrin and Metalloproteinase Domain Containing Protein 9 (ADAM9), Disintegrin and Metalloproteinase Domain Containing Disintegrin and Metalloproteinase Domain 5 Loproteinase (ADAMTS5), cathepsin B, cathepsin D, cathepsin E, cathepsin K, cathepsin L, cathepsin S, fibroblast activation protein alpha, hepsin, kallikrein-2, kallikrein-4, kallikrein-3, prostate specific antigen (PSA), kallikrein-13, legumain, matrix metallopeptidase 1 (MMP-1), matrix metallopeptidase 10 (MMP-10), matrix metal Lopeptidase 11 (MMP-11), Matrix Metallopeptidase 12 (MMP-12), Matrix Metallopeptidase 13 (MMP-13), Matrix Metallopeptidase 14 (MMP-14), Matrix Metallopeptidase 16 (MMP-16), Matrix Metallopeptidase 2 (MMP-2), Matrix Metallopeptidase 3 (MMP-3), Matrix Metallopeptidase 7 (MMP-7) ), matrix metallopeptidase 8 (MMP-8), matrix metallopeptidase 9 (MMP-9), matrix metallopeptidase 4 (MMP-4), matrix metallopeptidase 5 (MMP -5), matrix metallopeptidase 6 (MMP-6), matrix metallopeptidase 15 (MMP-15), neutrophil elastase, protease activated receptor 2 (PAR2), plasmin, prostacin, PSMA-FOLH1, membrane type serine protease 1 (MT-SP1), matriptase and u-plasminogen. In some embodiments, the mammalian protease is matrix metallopeptidase 1 (MMP1), matrix metallopeptidase 2 (MMP2), matrix metallopeptidase 7 (MMP7), matrix metallopeptidase 9 ( MMP9), matrix metallopeptidase 11 (MMP11), matrix metallopeptidase 14 (MMP14), urokinase-type plasminogen activator (uPA), legumain and matriptase. In some embodiments, a mammalian protease is preferentially expressed or activated in a target tissue or cell.

In some embodiments of methods for assessing the likelihood of a subject responding to a therapeutic agent, the target tissue or cell is a tumor. In some embodiments, the target tissue or cell produces or colocalizes with a mammalian protease.

In some embodiments of a method for assessing the likelihood of a subject responding to a therapeutic agent, a target tissue or cell contains or is associated with the reporter polypeptide in or on or proximate thereto. In some embodiments, the reporter polypeptide is a coagulation factor, complement component, tubulin, immunoglobulin, apolipoprotein, serum amyloid, insulin, growth factor, fibrinogen, PDZ domain protein, LIM domain protein, c-reactive protein, serum albumin, versican, collagen, elastin, keratin, kininogen-1, alpha-2-antiplasmin, clustererin, biglycan, alpha-1-antitrypsin, transthyretin, alpha-1-antichymotrypsin, Glucagon, hepcidin, thymosin beta-4, haptoglobin, hemoglobin subunit alpha, vesicle-associated protein 2, alpha-2-HS-glycoprotein, chromogranin-A, vitronectin, hemopexin, epididymal secreting sperm binding protein, secretogranin-2, angiotensinogen, transgelin-2, pancreatic prohormone, neurosecretory protein VGF, ceruloplasmin, PDZ and LIM domain protein 1, multimerin-1, inter-alpha- Trypsin inhibitor heavy chain H2, N-acetylmuramoyl-L-alanine amidase, histone H1.4, adhesion G-protein coupled receptor G6, mannan binding lectin serine protease 2, prothrombin, 1 protein deleted in malignant brain tumors (deleted in malignant brain tumors 1 protein), desmoglein-3, calcintenin-1, alpha-2-macroglobulin, myosin-9, sodium/potassium transport ATPase subunit gamma, oncoprotein-derived transcript 3 protein, serglycine, histidine rich glycoprotein, inter-alpha-trypsin inhibitor heavy chain H5, integrin alpha-IIb, membrane associated progesterone receptor component 1, histone H1.2, rho GDP-dissociation inhibitor 2, zinc-alpha-2-glycoprotein, Talin-1, Secretogranin-1, Neutrophil Defensin 3, Cytochrome P450 2E1, Gastric Inhibitory Polypeptide, Transcription Initiation Factor TFIID Subunit 1, Integral Membrane Protein 2B, Pigmented Epithelial Derived Factor, Voltage-dependent Type N Calcium Channel Subunit alpha-1B, ras GTPase-activating protein nGAP, type I cytoskeleton 17, sulfhydryl oxidase 1, homeobox protein Hox-B2, transcription factor SOX-10, E3 ubiquitin-protein ligase SIAH2, decorin, cysteine This is a polypeptide selected from the group consisting of secreted protein acidic and rich in cysteine (SPARC), laminin gamma 1 chain, vimentin and nidogen-1 (NID1). In some embodiments, the reporter polypeptide is versican, type II collagen alpha-1 chain, kininogen-1, complement C4-A, complement C4-B, complement C3, alpha-2-antiplasmin, clustererin , biglycan, elastin, fibrinogen alpha chain, alpha-1-antitrypsin, fibrinogen beta chain, type III collagen alpha-1 chain, serum amyloid A-1 protein, transthyretin, apolipoprotein AI, apolipoprotein AI iso Type 1, alpha-1-antichymotrypsin, glucagon, hepcidin, serum amyloid A-2 protein, thymosin beta-4, haptoglobin, hemoglobin subunit alpha, vesicle-associated protein 2, alpha-2-HS-sugar Protein, chromogranin-A, vitronectin, hemopexin, epididymal secreted sperm binding protein, direct skin, apolipoprotein C-III, secretogranin-2, angiotensinogen, c-reactive protein, serum albumin, Transgelin-2, pancreatic prohormone, neurosecretory protein VGF, ceruloplasmin, PDZ and LIM domain protein 1, tubulin alpha-4A chain, multimerin-1, inter-alpha-trypsin inhibitor heavy chain H2, apolipoprotein CI, fibrinogen gamma chain, N-acetylmuramoyl-L-alanine amidase, immunoglobulin lambda variable 3-21, histone H1.4, attachment G-protein coupled receptor G6, immunoglobulin lambda variable 3-25, immunoglobulin lambda Variable 1-51, immunoglobulin lambda variable 1-36, mannan-binding lectin serine protease 2, immunoglobulin kappa variable 3-20, immunoglobulin kappa variable 2-30, insulin-like growth factor II, apolipoprotein A-II, potential nonfunctional immunoglobulin kappa variable 2D-24, prothrombin, coagulation factor IX, apolipoprotein L1, protein 1 deleted in malignant brain tumor, desmoglein-3, calcintenin-1, immunoglobulin lambda constant 3, complement C5 , alpha-2-macroglobulin, myosin-9, sodium/potassium transport ATPase subunit gamma, immunoglobulin kappa variable 2-28, oncoprotein-derived transcript 3 protein, serglycine, coagulation factor XII, coagulation factor XIII A chain, insulin, histidine rich glycoprotein, immunoglobulin kappa variable 3-11, immunoglobulin kappa variable 1-39, collagen alpha-1(I) chain, inter-alpha-trypsin inhibitor heavy chain H5, potential transforming growth factor beta binding protein 2, Integrin alpha-IIb, membrane associated progesterone receptor component 1, immunoglobulin lambda variable 6-57, immunoglobulin kappa variable 3-15, complement C1r subcomponent-like protein, histone H1.2, Rho GDP-dissociation inhibitor 2, potential transforming growth Factor beta binding protein 4, collagen alpha-1 (XVIII) chain, immunoglobulin lambda variable 2-18, zinc-alpha-2-glycoprotein, talin-1, secretogranin-1, neutrophil defensin 3, cytochrome P450 2E1, Gastric Inhibitory Polypeptide, Immunoglobulin Heavy Chain Variable 3-15, Immunoglobulin Lambda Variable 2-11, Transcription Initiation Factor TFIID Subunit 1, Collagen Alpha-1 (VII) Chain, Integral Membrane Protein 2B, Pigmented Epithelial Derived Factor, Voltage dependent type N calcium channel subunit alpha-1B, immunoglobulin lambda variable 3-27, ras GTPase-activating protein nGAP, keratin, type I cytoskeleton 17, tubulin beta chain, sulfhydryl oxidase 1, immunoglobulin kappa variable 4-1, complement C1r subcomponent, homeobox protein Hox-B2, transcription factor SOX-10, E3 ubiquitin-protein ligase SIAH2, decorin, SPARC, type I collagen alpha-1 chain, type IV collagen alpha-1 chain, laminin gamma 1 chain, vimentin, collagen type III, collagen type IV alpha-3 chain, collagen type VII alpha-1 chain, collagen type VI alpha-1 chain, collagen type V alpha-1 chain, nidogen-1 and type VI collagen alpha-3 chains. In some embodiments, the reporter polypeptide comprises a sequence set forth in columns II-VI of Table A (or a subset thereof). In some embodiments, the reporter polypeptide is selected from the group set forth in column I of Table A (or a subset thereof).

In some embodiments of methods for assessing the likelihood of a subject responding to a therapeutic agent, the target tissue or cell is characterized by an increased amount or activity of a mammalian protease proximal to the target tissue or cell compared to a non-target tissue or cell of the subject. to be In some embodiments, the subject suffers from or is suspected of suffering from a disease or condition characterized by increased expression or activity of a mammalian protease proximal to a target tissue or cell compared to a corresponding non-target tissue or cell of the subject.

In some embodiments of the method for assessing the likelihood of a subject responding to a therapeutic agent, the disease or condition is cancer or an inflammatory or autoimmune disease. In some embodiments, the disease or condition is carcinoma, Hodgkin's lymphoma and non-Hodgkin's lymphoma, diffuse large B-cell lymphoma, follicular lymphoma, mantle cell lymphoma, blastoma, breast cancer, ER/PR+ breast cancer, Her2+ breast cancer, triple negative breast cancer, colon Cancer, colorectal cancer with malignant ascites, mucinous tumor, prostate cancer, head and neck cancer, skin cancer, melanoma, genitourinary cancer, ovarian cancer, ovarian cancer with malignant ascites, peritoneal carcinomatosis, uterine serous carcinoma, endometrium Cancer, cervical cancer, colorectal cancer, uterine cancer, peritoneal mesothelioma, kidney cancer, Wilms' tumor, lung cancer, small cell lung cancer, non-small cell lung cancer, gastric cancer, stomach cancer, small intestine cancer, liver cancer, hepatocarcinoma, hepatoblastoma, fat sarcomas, pancreatic cancers, gallbladder cancers, cholangiocarcinomas, esophageal cancers, salivary gland carcinomas, thyroid cancers, epithelial cancers, male germ cell tumors, adenocarcinomas, sarcomas, and chronic lymphocytic leukemia of B-cell origin. In some embodiments, the disease or condition is ankylosing spondylitis (AS), arthritis (e.g., rheumatoid arthritis (RA), juvenile idiopathic arthritis (JIA), osteoarthritis (OA), psoriatic arthritis (PsA), gout, chronic arthritis, but not limited to), Chagas disease, chronic obstructive pulmonary disease (COPD), dermatomyositis, type 1 diabetes, endometriosis, Goodpasture syndrome, Graves disease, Guillain-Barré syndrome (GBS), Hashimoto's disease, purulent scab, Kawasaki disease, IgA nephropathy, idiopathic thrombocytopenic purpura, inflammatory bowel disease (IBD) (eg, Crohn's disease (CD), clonal disease, ulcerative colitis, collagenous colitis, lymphocytic colitis, ischemic colitis, empty colitis, Behcet's syndrome, infectious colitis, indeterminate colitis, interstitial cystitis, but not limited to) lupus (eg, systemic lupus erythematosus, discoid lupus, subacute cutaneous lupus erythematosus, cutaneous lupus erythematosus ( (e.g., alumni lupus erythematosus), drug-induced lupus, neonatal lupus, lupus nephritis (but not limited to), mixed connective tissue disease, focal scleroderma, multiple sclerosis (MS), severe muscular dystrophy, narcolepsy, neuromuscular angina, Pemphigus vulgaris, pernicious anemia, psoriasis, psoriatic arthritis, polymyositis, primary biliary cirrhosis, relapsing polychondritis, schizophrenia, scleroderma, Sjogren's syndrome, systemic stiffness syndrome, temporal arteritis (also called giant cell arteritis), and vasculitis , vitiligo, Wegener's granulomatosis, immune response associated with transplant rejection (eg, but not limited to, kidney transplant rejection, lung transplant rejection, liver transplant rejection), psoriasis, Wiskott-Aldrich syndrome, autoimmune lymphoproliferative syndrome, Myasthenia gravis, inflammatory chronic rhinosinusitis, colitis, chronic digestive disorder, Barrett's esophagus, inflammatory gastritis, autoimmune nephritis, autoimmune hepatitis, autoimmune carditis, autoimmune encephalitis, autoimmune mediated blood disorders, asthma, atopic dermatitis , Atopy, allergy, allergic rhinitis, scleroderma, bronchitis, selected from the group consisting of pericarditis, inflammatory diseases are Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis, inflammatory lung disease, inflammatory skin disease, atherosclerosis, myocardial infarction , stroke, gram-positive shock, gram-negative shock, sepsis, septic shock, hemorrhagic shock, anaphylactic shock, and systemic inflammatory response syndrome.

In some embodiments of the method for assessing the likelihood that a subject will respond to a therapeutic agent, the therapeutic agent is an anti-cancer agent. In some embodiments, the therapeutic agent is an activatable therapeutic agent. In some embodiments, the therapeutic agent is an activatable therapeutic agent, or a non-natural activatable therapeutic agent as described herein.

In some embodiments of the method for assessing the likelihood that a subject will respond to a therapeutic agent, the therapeutic agent further comprises a masking moiety (MM). In some embodiments of methods for assessing the likelihood of a subject responding to a therapeutic agent, the masking moiety (MM) can be released from the therapeutic agent upon cleavage of the peptide substrate by a mammalian protease. In some embodiments, the masking moiety (MM), in its uncleaved state, interferes with the therapeutic agent's interaction with the target tissue or cell. In some embodiments, the bioactivity of a therapeutic agent may be enhanced upon cleavage of the peptide substrate by a mammalian protease. In some embodiments, the masking moiety (MM) is an extended recombinant polypeptide (XTEN). In some embodiments, an XTEN is characterized by: (i) comprises at least 100 amino acids; (ii) at least 90% of the amino acid residues are selected from glycine (G), alanine (A), serine (S), threonine (T), glutamate (E) and proline (P); (iii) at least four different types of amino acids selected from G, A, S, T, E and P.

In some embodiments of the method for assessing the likelihood that a subject will respond to a therapeutic agent, the method further comprises transmitting the assignment details to a health care provider and/or to the subject.

In some embodiments of a method for assessing the likelihood of a subject responding to a therapeutic agent, the method further comprises (b) thereafter contacting the therapeutic agent with a mammalian protease.

In some embodiments of the method for assessing the likelihood that a subject will respond to a therapeutic agent, after (b), further comprising administering to the subject an effective amount of the therapeutic agent based on the specifications in step (b).

In some embodiments of a method for assessing the likelihood of a subject responding to a therapeutic agent, (a) comprises detecting the polypeptide of (i), (ii) or (iii) in an immunoassay. In some embodiments, the immunoassay uses an antibody that specifically binds to the polypeptide of (i), (ii) or (iii) or an epitope thereof.

In some embodiments of a method for assessing the likelihood of a subject responding to a therapeutic agent, (a) is a polypeptide (or derivative (fragment ( s) including)).

In some embodiments of the methods, use of a diagnostic reagent to assess the likelihood of a subject suffering from a disease or disorder responding to a therapeutic agent that can be activated by a mammalian protease expressed in the subject is provided.

In certain embodiments, diagnostic reagents are used to assess the likelihood that a subject suffering from a disease or disorder will respond to a therapeutic agent that can be activated by a mammalian protease expressed in the subject.

In some embodiments, a mammalian protease capable of being activated by a mammalian protease expressed in a subject suffering from a disease or disorder, comprising a reagent for detecting the presence or amount of a proteolytic peptide product produced by the action of the mammalian protease. Kits for practicing methods for assessing the likelihood that a subject will respond to a therapeutic agent are provided.

In certain aspects, the present disclosure provides a method of treating a subject in need of a therapeutic agent capable of being activated by a mammalian protease expressed in the subject, the method comprising

Administering an effective amount of a therapeutic agent to a subject, wherein the subject has been shown to express in a biological sample from the subject:

(i) a polypeptide comprising at least 5, at least 6, at least 7, at least 8, at least 9 or at least 10 contiguous amino acid residues represented in the sequence set forth in column V of Table A (or a subset thereof); or

(ii) a polypeptide comprising at least 5, at least 6, at least 7, at least 8, at least 9 or at least 10 contiguous amino acids shown in the sequence set forth in column IV (or a subset thereof) of Table A ; or

(iii) a polypeptide comprising at least 5, at least 6, at least 7, at least 8, at least 9 or at least 10 contiguous amino acids shown in the sequence set forth in column VI of Table A (or a subset thereof); or

(iv) The expression level of polypeptide (i), (ii) or (iii) exceeds a threshold value.

In some embodiments for treating a subject with a therapeutic agent, the polypeptide of ( i ) comprises at least 6 , at least 7, at least 8, at least 9, or It contains at least 10 contiguous amino acid residues. In some embodiments, the polypeptide of (ii) comprises at least 6, at least 7, at least 8, at least 9 or at least 10 contiguous amino acids indicated in the sequence set forth in column IV of Table A (or a subset thereof). do. In some embodiments, the polypeptide of (iii) comprises at least 6, at least 7, at least 8, at least 9 or at least 10 contiguous amino acids indicated in the sequence set forth in column VI of Table A (or a subset thereof). do. In some embodiments, the subject has been shown to express any two of (i) to (iii) in a biological sample. In some embodiments, the subject has been shown to express all three of (i) to (iii) in a biological sample.

In some embodiments for treating a subject with a therapeutic agent, the therapeutic agent comprises a peptide substrate susceptible to cleavage by mammalian proteases. In some embodiments, the peptide substrate is susceptible to cleavage by a mammalian protease at the cleavable linkage, wherein the polypeptide of (i), (ii) or (iii) is at the N-terminus or C-terminus of the cleavable linkage. It includes a portion comprising at least 4 contiguous amino acid residues of a phosphorus peptide substrate. In some embodiments, the portion of the peptide substrate that is the N-terminus of the scissile bond is the C-terminus containing 4 to 10 amino acid residues of the sequence set forth in column IV or V of Table A (or a subset thereof). up to 3 or 2 amino acid substitutions or up to 1 amino acid substitution relative to the sequence at the end, wherein none of the amino acid substitutions are at positions corresponding to amino acid residues immediately adjacent to the corresponding scissile bond. In some embodiments, the portion of the peptide substrate that is N-terminal of the scissile bond is a sequence at the C-terminal end containing 4 to 10 amino acid residues of the sequence set forth in column IV of Table A (or a subset thereof). up to 3 or 2 amino acid substitutions or up to 1 amino acid substitution for , wherein none of the amino acid substitutions is at a position corresponding to an amino acid residue immediately adjacent to the corresponding scissile bond. In some embodiments, the portion of the peptide substrate that is N-terminal of the scissile bond is a sequence at the C-terminal end containing 4 to 10 amino acid residues of the sequence set forth in column V of Table A (or a subset thereof). up to 3 or 2 amino acid substitutions or up to 1 amino acid substitution for , wherein none of the amino acid substitutions is at a position corresponding to an amino acid residue immediately adjacent to the corresponding scissile bond. In some embodiments, the portion of the peptide substrate that is the N-terminus of the scissile bond is the C-terminus containing 4 to 10 amino acid residues of the sequence set forth in column IV or V of Table A (or a subset thereof). contains the sequence of the end. In some embodiments, the portion of the peptide substrate that is N-terminal of the scissile bond is a sequence at the C-terminal end containing 4 to 10 amino acid residues of the sequence set forth in column IV of Table A (or a subset thereof). includes In some embodiments, the portion of the peptide substrate that is N-terminal of the scissile bond is a sequence at the C-terminal end containing 4 to 10 amino acid residues of the sequence set forth in column V of Table A (or a subset thereof). includes In some embodiments, the portion of the peptide substrate that is the C-terminus of the scissile bond is the N-terminus containing 4 to 10 amino acid residues of the sequence set forth in column V or column VI (or a subset thereof) of Table A. up to 3 or 2 amino acid substitutions or up to 1 amino acid substitution relative to the sequence at the end, wherein none of the amino acid substitutions are at positions corresponding to amino acid residues immediately adjacent to the corresponding scissile bond. In some embodiments, the portion of the peptide substrate that is C-terminal of the scissile bond is a sequence at the N-terminal end containing 4 to 10 amino acid residues of the sequence set forth in column V of Table A (or a subset thereof). up to 3 or 2 amino acid substitutions or up to 1 amino acid substitution for , wherein none of the amino acid substitutions is at a position corresponding to an amino acid residue immediately adjacent to the corresponding scissile bond. In some embodiments, the portion of the peptide substrate that is the C-terminus of the scissile bond is a sequence at the N-terminal end containing 4 to 10 amino acid residues of the sequence set forth in column VI of Table A (or a subset thereof). up to 3 or 2 amino acid substitutions or up to 1 amino acid substitution for , wherein none of the amino acid substitutions is at a position corresponding to an amino acid residue immediately adjacent to the corresponding scissile bond. In some embodiments, the portion of the peptide substrate that is the C-terminus of the scissile bond is the N-terminus containing 4 to 10 amino acid residues of the sequence set forth in column V or column VI (or a subset thereof) of Table A. contains the sequence of the end. In some embodiments, the portion of the peptide substrate that is C-terminal of the scissile bond is a sequence at the N-terminal end containing 4 to 10 amino acid residues of the sequence set forth in column V of Table A (or a subset thereof). includes In some embodiments, the portion of the peptide substrate that is the C-terminus of the scissile bond is a sequence at the N-terminal end containing 4 to 10 amino acid residues of the sequence set forth in column VI of Table A (or a subset thereof). includes

In some embodiments for treating a subject with a therapeutic agent, the threshold is zero or a nominal threshold. In some embodiments, a biological sample includes a serum or plasma sample. In some embodiments, a biological sample comprises a serum sample. In some embodiments, a biological sample comprises a plasma sample.

In some embodiments for treating a subject with a therapeutic agent, the mammalian protease is a serine protease, a cysteine protease, an aspartate protease, a threonine protease, or a metalloproteinase. In some embodiments, the mammalian protease is disintegrin and metalloproteinase domain containing protein 10 (ADAM10), disintegrin and metalloproteinase domain containing protein 12 (ADAM12), disintegrin and metalloproteinase domain containing Protein 15 (ADAM15), Disintegrin and Metalloproteinase Domain Containing Protein 17 (ADAM17), Disintegrin and Metalloproteinase Domain Containing Protein 9 (ADAM9), Disintegrin and Metalloproteinase Domain Containing Disintegrin and Metalloproteinase Domain 5 Loproteinase (ADAMTS5), cathepsin B, cathepsin D, cathepsin E, cathepsin K, cathepsin L, cathepsin S, fibroblast activation protein alpha, hepsin, kallikrein-2, kallikrein-4, kallikrein-3, prostate specific antigen (PSA), kallikrein-13, legumain, matrix metallopeptidase 1 (MMP-1), matrix metallopeptidase 10 (MMP-10), matrix metal Lopeptidase 11 (MMP-11), Matrix Metallopeptidase 12 (MMP-12), Matrix Metallopeptidase 13 (MMP-13), Matrix Metallopeptidase 14 (MMP-14), Matrix Metallopeptidase 16 (MMP-16), Matrix Metallopeptidase 2 (MMP-2), Matrix Metallopeptidase 3 (MMP-3), Matrix Metallopeptidase 7 (MMP-7) ), matrix metallopeptidase 8 (MMP-8), matrix metallopeptidase 9 (MMP-9), matrix metallopeptidase 4 (MMP-4), matrix metallopeptidase 5 (MMP -5), matrix metallopeptidase 6 (MMP-6), matrix metallopeptidase 15 (MMP-15), neutrophil elastase, protease activated receptor 2 (PAR2), plasmin, prostacin, PSMA-FOLH1, membrane type serine protease 1 (MT-SP1), matriptase and u-plasminogen. In some embodiments, the mammalian protease is matrix metallopeptidase 1 (MMP1), matrix metallopeptidase 2 (MMP2), matrix metallopeptidase 7 (MMP7), matrix metallopeptidase 9 ( MMP9), matrix metallopeptidase 11 (MMP11), matrix metallopeptidase 14 (MMP14), urokinase-type plasminogen activator (uPA), legumain and matriptase. In some embodiments, a mammalian protease is preferentially expressed or activated in a target tissue or cell. In some embodiments, the target tissue or cell is a tumor. In some embodiments, the target tissue or cell produces or colocalizes with a mammalian protease.

In some embodiments for treating a subject with a therapeutic agent, the target tissue or cell contains or is associated with the reporter polypeptide in or on or proximal thereto. In some embodiments, the reporter polypeptide is a coagulation factor, complement component, tubulin, immunoglobulin, apolipoprotein, serum amyloid, insulin, growth factor, fibrinogen, PDZ domain protein, LIM domain protein, c-reactive protein, serum albumin, versican, collagen, elastin, keratin, kininogen-1, alpha-2-antiplasmin, clustererin, biglycan, alpha-1-antitrypsin, transthyretin, alpha-1-antichymotrypsin, Glucagon, hepcidin, thymosin beta-4, haptoglobin, hemoglobin subunit alpha, vesicle-associated protein 2, alpha-2-HS-glycoprotein, chromogranin-A, vitronectin, hemopexin, epididymal secreting sperm binding protein, secretogranin-2, angiotensinogen, transgelin-2, pancreatic prohormone, neurosecretory protein VGF, ceruloplasmin, PDZ and LIM domain protein 1, multimerin-1, inter-alpha- Trypsin inhibitor heavy chain H2, N-acetylmuramoyl-L-alanine amidase, histone H1.4, adhesion G-protein coupled receptor G6, mannan binding lectin serine protease 2, prothrombin, 1 protein deleted in malignant brain tumors (deleted in malignant brain tumors 1 protein), desmoglein-3, calcintenin-1, alpha-2-macroglobulin, myosin-9, sodium/potassium transport ATPase subunit gamma, oncoprotein-derived transcript 3 protein, serglycine, histidine rich glycoprotein, inter-alpha-trypsin inhibitor heavy chain H5, integrin alpha-IIb, membrane associated progesterone receptor component 1, histone H1.2, rho GDP-dissociation inhibitor 2, zinc-alpha-2-glycoprotein, Talin-1, Secretogranin-1, Neutrophil Defensin 3, Cytochrome P450 2E1, Gastric Inhibitory Polypeptide, Transcription Initiation Factor TFIID Subunit 1, Integral Membrane Protein 2B, Pigmented Epithelial Derived Factor, Voltage-dependent Type N Calcium Channel Subunit alpha-1B, ras GTPase-activating protein nGAP, type I cytoskeleton 17, sulfhydryl oxidase 1, homeobox protein Hox-B2, transcription factor SOX-10, E3 ubiquitin-protein ligase SIAH2, decorin, cysteine This is a polypeptide selected from the group consisting of secreted protein acidic and rich in cysteine (SPARC), laminin gamma 1 chain, vimentin and nidogen-1 (NID1). In some embodiments, the reporter polypeptide is versican, type II collagen alpha-1 chain, kininogen-1, complement C4-A, complement C4-B, complement C3, alpha-2-antiplasmin, clustererin , biglycan, elastin, fibrinogen alpha chain, alpha-1-antitrypsin, fibrinogen beta chain, type III collagen alpha-1 chain, serum amyloid A-1 protein, transthyretin, apolipoprotein AI, apolipoprotein AI iso Type 1, alpha-1-antichymotrypsin, glucagon, hepcidin, serum amyloid A-2 protein, thymosin beta-4, haptoglobin, hemoglobin subunit alpha, vesicle-associated protein 2, alpha-2-HS-sugar Protein, chromogranin-A, vitronectin, hemopexin, epididymal secreted sperm binding protein, direct skin, apolipoprotein C-III, secretogranin-2, angiotensinogen, c-reactive protein, serum albumin, Transgelin-2, pancreatic prohormone, neurosecretory protein VGF, ceruloplasmin, PDZ and LIM domain protein 1, tubulin alpha-4A chain, multimerin-1, inter-alpha-trypsin inhibitor heavy chain H2, apolipoprotein CI, fibrinogen gamma chain, N-acetylmuramoyl-L-alanine amidase, immunoglobulin lambda variable 3-21, histone H1.4, attachment G-protein coupled receptor G6, immunoglobulin lambda variable 3-25, immunoglobulin lambda Variable 1-51, immunoglobulin lambda variable 1-36, mannan-binding lectin serine protease 2, immunoglobulin kappa variable 3-20, immunoglobulin kappa variable 2-30, insulin-like growth factor II, apolipoprotein A-II, potential nonfunctional immunoglobulin kappa variable 2D-24, prothrombin, coagulation factor IX, apolipoprotein L1, protein 1 deleted in malignant brain tumor, desmoglein-3, calcintenin-1, immunoglobulin lambda constant 3, complement C5 , alpha-2-macroglobulin, myosin-9, sodium/potassium transport ATPase subunit gamma, immunoglobulin kappa variable 2-28, oncoprotein-derived transcript 3 protein, serglycine, coagulation factor XII, coagulation factor XIII A chain, insulin, histidine rich glycoprotein, immunoglobulin kappa variable 3-11, immunoglobulin kappa variable 1-39, collagen alpha-1(I) chain, inter-alpha-trypsin inhibitor heavy chain H5, potential transforming growth factor beta binding protein 2, Integrin alpha-IIb, membrane associated progesterone receptor component 1, immunoglobulin lambda variable 6-57, immunoglobulin kappa variable 3-15, complement C1r subcomponent-like protein, histone H1.2, Rho GDP-dissociation inhibitor 2, potential transforming growth Factor beta binding protein 4, collagen alpha-1 (XVIII) chain, immunoglobulin lambda variable 2-18, zinc-alpha-2-glycoprotein, talin-1, secretogranin-1, neutrophil defensin 3, cytochrome P450 2E1, Gastric Inhibitory Polypeptide, Immunoglobulin Heavy Chain Variable 3-15, Immunoglobulin Lambda Variable 2-11, Transcription Initiation Factor TFIID Subunit 1, Collagen Alpha-1 (VII) Chain, Integral Membrane Protein 2B, Pigmented Epithelial Derived Factor, Voltage dependent type N calcium channel subunit alpha-1B, immunoglobulin lambda variable 3-27, ras GTPase-activating protein nGAP, keratin, type I cytoskeleton 17, tubulin beta chain, sulfhydryl oxidase 1, immunoglobulin kappa variable 4-1, complement C1r subcomponent, homeobox protein Hox-B2, transcription factor SOX-10, E3 ubiquitin-protein ligase SIAH2, decorin, SPARC, type I collagen alpha-1 chain, type IV collagen alpha-1 chain, laminin gamma 1 chain, vimentin, collagen type III, collagen type IV alpha-3 chain, collagen type VII alpha-1 chain, collagen type VI alpha-1 chain, collagen type V alpha-1 chain, nidogen-1 and type VI collagen alpha-3 chains. In some embodiments, the reporter polypeptide comprises a sequence set forth in columns II-VI of Table A (or a subset thereof). In some embodiments, the reporter polypeptide is selected from the group set forth in column I of Table A (or a subset thereof).

In some embodiments for treating a subject with a therapeutic agent, the target tissue or cell is characterized by an increased amount or activity of a mammalian protease proximal to the target tissue or cell compared to a non-target tissue or cell of the subject. In some embodiments, the subject suffers from or is suspected of suffering from a disease or condition characterized by increased expression or activity of a mammalian protease proximal to a target tissue or cell compared to a corresponding non-target tissue or cell of the subject. In some embodiments, the disease or condition is cancer or an inflammatory or autoimmune disease. In some embodiments, the disease or condition is ankylosing spondylitis (AS), arthritis (e.g., rheumatoid arthritis (RA), juvenile idiopathic arthritis (JIA), osteoarthritis (OA), psoriatic arthritis (PsA), gout, chronic arthritis, but not limited to), Chagas disease, chronic obstructive pulmonary disease (COPD), dermatomyositis, type 1 diabetes, endometriosis, Goodpasture syndrome, Graves disease, Guillain-Barré syndrome (GBS), Hashimoto's disease, purulent scab, Kawasaki disease, IgA nephropathy, idiopathic thrombocytopenic purpura, inflammatory bowel disease (IBD) (eg, Crohn's disease (CD), clonal disease, ulcerative colitis, collagenous colitis, lymphocytic colitis, ischemic colitis, empty colitis, Behcet's syndrome, infectious colitis, indeterminate colitis, interstitial cystitis, but not limited to) lupus (eg, systemic lupus erythematosus, discoid lupus, subacute cutaneous lupus erythematosus, cutaneous lupus erythematosus ( (e.g., alumni lupus erythematosus), drug-induced lupus, neonatal lupus, lupus nephritis (but not limited to), mixed connective tissue disease, focal scleroderma, multiple sclerosis (MS), severe muscular dystrophy, narcolepsy, neuromuscular angina, Pemphigus vulgaris, pernicious anemia, psoriasis, psoriatic arthritis, polymyositis, primary biliary cirrhosis, relapsing polychondritis, schizophrenia, scleroderma, Sjogren's syndrome, systemic stiffness syndrome, temporal arteritis (also called giant cell arteritis), and vasculitis , vitiligo, Wegener's granulomatosis, immune response associated with transplant rejection (eg, but not limited to, kidney transplant rejection, lung transplant rejection, liver transplant rejection), psoriasis, Wiskott-Aldrich syndrome, autoimmune lymphoproliferative syndrome, Myasthenia gravis, inflammatory chronic rhinosinusitis, colitis, chronic digestive disorder, Barrett's esophagus, inflammatory gastritis, autoimmune nephritis, autoimmune hepatitis, autoimmune carditis, autoimmune encephalitis, autoimmune mediated blood disorders, asthma, atopic dermatitis , Atopy, allergy, allergic rhinitis, scleroderma, bronchitis, selected from the group consisting of pericarditis, inflammatory diseases are Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis, inflammatory lung disease, inflammatory skin disease, atherosclerosis, myocardial infarction , stroke, gram-positive shock, gram-negative shock, sepsis, septic shock, hemorrhagic shock, anaphylactic shock, and systemic inflammatory response syndrome. In some embodiments, the disease or condition is carcinoma, Hodgkin's lymphoma and non-Hodgkin's lymphoma, diffuse large B-cell lymphoma, follicular lymphoma, mantle cell lymphoma, blastoma, breast cancer, ER/PR+ breast cancer, Her2+ breast cancer, triple negative breast cancer, colon Cancer, colorectal cancer with malignant ascites, mucinous tumor, prostate cancer, head and neck cancer, skin cancer, melanoma, genitourinary cancer, ovarian cancer, ovarian cancer with malignant ascites, peritoneal carcinomatosis, uterine serous carcinoma, endometrium Cancer, cervical cancer, colorectal cancer, uterine cancer, peritoneal mesothelioma, kidney cancer, Wilms' tumor, lung cancer, small cell lung cancer, non-small cell lung cancer, gastric cancer, stomach cancer, small intestine cancer, liver cancer, hepatocarcinoma, hepatoblastoma, fat sarcomas, pancreatic cancers, gallbladder cancers, cholangiocarcinomas, esophageal cancers, salivary gland carcinomas, thyroid cancers, epithelial cancers, male germ cell tumors, adenocarcinomas, sarcomas, and chronic lymphocytic leukemia of B-cell origin. In some embodiments, the therapeutic agent is an anti-cancer agent. In some embodiments, the therapeutic agent is an activatable therapeutic agent. In some embodiments, the therapeutic agent is a non-natural, activatable therapeutic agent as described herein.

In some embodiments for treating a subject with a therapeutic agent, the therapeutic agent comprises a masking moiety (MM). In some embodiments, the masking moiety (MM) can be released from the therapeutic upon cleavage of the peptide substrate by a mammalian protease. In some embodiments, the masking moiety (MM), in its uncleaved state, interferes with the therapeutic agent's interaction with the target tissue or cell. In some embodiments, the bioactivity of a therapeutic agent may be enhanced upon cleavage of the peptide substrate by a mammalian protease. In some embodiments, the masking moiety (MM) is an extended recombinant polypeptide (XTEN). In some embodiments, an XTEN is characterized by: (i) comprises at least 100 amino acids; (ii) at least 90% of the amino acid residues are selected from glycine (G), alanine (A), serine (S), threonine (T), glutamate (E) and proline (P); (iii) at least four different types of amino acids selected from G, A, S, T, E and P.

In some embodiments for treating a subject with a therapeutic agent, the subject is determined to have a potential response to the therapeutic agent by a method as described herein.

In certain embodiments, the present disclosure provides treatment of a disease or condition in a subject in need thereof, comprising administering to a subject in need thereof one or more therapeutically effective doses of a therapeutic agent as described herein or a pharmaceutical composition as described herein. provides a way to

In some embodiments of the method of treating a disease or condition in a subject, the subject is selected from the group consisting of mouse, rat, monkey, and human. In some embodiments, the subject is a human. In some embodiments, the subject is determined to have a potential response to a therapeutic agent or pharmaceutical composition. In some embodiments, the probability of reaction is greater than 50%. In some embodiments, the likelihood of a reaction is determined by a method as described herein.

In some embodiments of the method of treating a disease or condition in a subject, the disease or condition is cancer or an inflammatory or autoimmune disease. In some embodiments, the disease or condition is ankylosing spondylitis (AS), arthritis (e.g., rheumatoid arthritis (RA), juvenile idiopathic arthritis (JIA), osteoarthritis (OA), psoriatic arthritis (PsA), gout, chronic arthritis, but not limited to), Chagas disease, chronic obstructive pulmonary disease (COPD), dermatomyositis, type 1 diabetes, endometriosis, Goodpasture syndrome, Graves disease, Guillain-Barré syndrome (GBS), Hashimoto's disease, purulent scab, Kawasaki disease, IgA nephropathy, idiopathic thrombocytopenic purpura, inflammatory bowel disease (IBD) (eg, Crohn's disease (CD), clonal disease, ulcerative colitis, collagenous colitis, lymphocytic colitis, ischemic colitis, empty colitis, Behcet's syndrome, infectious colitis, indeterminate colitis, interstitial cystitis, but not limited to) lupus (eg, systemic lupus erythematosus, discoid lupus, subacute cutaneous lupus erythematosus, cutaneous lupus erythematosus ( (e.g., alumni lupus erythematosus), drug-induced lupus, neonatal lupus, lupus nephritis (but not limited to), mixed connective tissue disease, focal scleroderma, multiple sclerosis (MS), severe muscular dystrophy, narcolepsy, neuromuscular angina, Pemphigus vulgaris, pernicious anemia, psoriasis, psoriatic arthritis, polymyositis, primary biliary cirrhosis, relapsing polychondritis, schizophrenia, scleroderma, Sjogren's syndrome, systemic stiffness syndrome, temporal arteritis (also called giant cell arteritis), and vasculitis , vitiligo, Wegener's granulomatosis, immune response associated with transplant rejection (eg, but not limited to, kidney transplant rejection, lung transplant rejection, liver transplant rejection), psoriasis, Wiskott-Aldrich syndrome, autoimmune lymphoproliferative syndrome, Myasthenia gravis, inflammatory chronic rhinosinusitis, colitis, chronic digestive disorder, Barrett's esophagus, inflammatory gastritis, autoimmune nephritis, autoimmune hepatitis, autoimmune carditis, autoimmune encephalitis, autoimmune mediated blood disorders, asthma, atopic dermatitis , Atopy, allergy, allergic rhinitis, scleroderma, bronchitis, selected from the group consisting of pericarditis, inflammatory diseases are Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis, inflammatory lung disease, inflammatory skin disease, atherosclerosis, myocardial infarction , stroke, gram-positive shock, gram-negative shock, sepsis, septic shock, hemorrhagic shock, anaphylactic shock, and systemic inflammatory response syndrome. In some embodiments, the disease or condition is carcinoma, Hodgkin's lymphoma and non-Hodgkin's lymphoma, diffuse large B-cell lymphoma, follicular lymphoma, mantle cell lymphoma, blastoma, breast cancer, ER/PR+ breast cancer, Her2+ breast cancer, triple negative breast cancer, colon Cancer, colorectal cancer with malignant ascites, mucinous tumor, prostate cancer, head and neck cancer, skin cancer, melanoma, genitourinary cancer, ovarian cancer, ovarian cancer with malignant ascites, peritoneal carcinomatosis, uterine serous carcinoma, endometrium Cancer, cervical cancer, colorectal cancer, uterine cancer, peritoneal mesothelioma, kidney cancer, Wilms' tumor, lung cancer, small cell lung cancer, non-small cell lung cancer, gastric cancer, stomach cancer, small intestine cancer, liver cancer, hepatocarcinoma, hepatoblastoma, fat sarcomas, pancreatic cancers, gallbladder cancers, cholangiocarcinomas, esophageal cancers, salivary gland carcinomas, thyroid cancers, epithelial cancers, male germ cell tumors, adenocarcinomas, sarcomas, and chronic lymphocytic leukemia of B-cell origin.

In certain embodiments, the present disclosure provides use of a therapeutic agent as described herein in the manufacture of a medicament for the treatment of a disease or condition in a subject.

In certain aspects, the present disclosure provides use of a pharmaceutical composition as described herein in the manufacture of a medicament for the treatment of a disease or condition in a subject.

In some embodiments of use, the subject is selected from the group consisting of mouse, rat, monkey and human. In some embodiments, the subject is a human. In some embodiments, the subject is determined to have a potential response to a therapeutic agent or pharmaceutical composition. In some embodiments, the probability of reaction is greater than 50%. In some embodiments, the likelihood of a reaction is determined by a method as described herein.

In some embodiments of use, the disease or condition is cancer or an inflammatory or autoimmune disease. In some embodiments, the disease or condition is carcinoma, Hodgkin's lymphoma and non-Hodgkin's lymphoma, diffuse large B-cell lymphoma, follicular lymphoma, mantle cell lymphoma, blastoma, breast cancer, ER/PR+ breast cancer, Her2+ breast cancer, triple negative breast cancer, colon Cancer, colorectal cancer with malignant ascites, mucinous tumor, prostate cancer, head and neck cancer, skin cancer, melanoma, genitourinary cancer, ovarian cancer, ovarian cancer with malignant ascites, peritoneal carcinomatosis, uterine serous carcinoma, endometrium Cancer, cervical cancer, colorectal cancer, uterine cancer, peritoneal mesothelioma, kidney cancer, Wilms' tumor, lung cancer, small cell lung cancer, non-small cell lung cancer, gastric cancer, stomach cancer, small intestine cancer, liver cancer, hepatocarcinoma, hepatoblastoma, fat sarcomas, pancreatic cancers, gallbladder cancers, cholangiocarcinomas, esophageal cancers, salivary gland carcinomas, thyroid cancers, epithelial cancers, male germ cell tumors, adenocarcinomas, sarcomas, and chronic lymphocytic leukemia of B-cell origin. In some embodiments, the disease or condition is ankylosing spondylitis (AS), arthritis (e.g., rheumatoid arthritis (RA), juvenile idiopathic arthritis (JIA), osteoarthritis (OA), psoriatic arthritis (PsA), gout, chronic arthritis, but not limited to), Chagas disease, chronic obstructive pulmonary disease (COPD), dermatomyositis, type 1 diabetes, endometriosis, Goodpasture syndrome, Graves disease, Guillain-Barré syndrome (GBS), Hashimoto's disease, purulent scab, Kawasaki disease, IgA nephropathy, idiopathic thrombocytopenic purpura, inflammatory bowel disease (IBD) (eg, Crohn's disease (CD), clonal disease, ulcerative colitis, collagenous colitis, lymphocytic colitis, ischemic colitis, empty colitis, Behcet's syndrome, infectious colitis, indeterminate colitis, interstitial cystitis, but not limited to) lupus (eg, systemic lupus erythematosus, discoid lupus, subacute cutaneous lupus erythematosus, cutaneous lupus erythematosus ( (e.g., alumni lupus erythematosus), drug-induced lupus, neonatal lupus, lupus nephritis (but not limited to), mixed connective tissue disease, focal scleroderma, multiple sclerosis (MS), severe muscular dystrophy, narcolepsy, neuromuscular angina, Pemphigus vulgaris, pernicious anemia, psoriasis, psoriatic arthritis, polymyositis, primary biliary cirrhosis, relapsing polychondritis, schizophrenia, scleroderma, Sjogren's syndrome, systemic stiffness syndrome, temporal arteritis (also called giant cell arteritis), and vasculitis , vitiligo, Wegener's granulomatosis, immune response associated with transplant rejection (eg, but not limited to, kidney transplant rejection, lung transplant rejection, liver transplant rejection), psoriasis, Wiskott-Aldrich syndrome, autoimmune lymphoproliferative syndrome, Myasthenia gravis, inflammatory chronic rhinosinusitis, colitis, chronic digestive disorder, Barrett's esophagus, inflammatory gastritis, autoimmune nephritis, autoimmune hepatitis, autoimmune carditis, autoimmune encephalitis, autoimmune mediated blood disorders, asthma, atopic dermatitis , Atopy, allergy, allergic rhinitis, scleroderma, bronchitis, selected from the group consisting of pericarditis, inflammatory diseases are Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis, inflammatory lung disease, inflammatory skin disease, atherosclerosis, myocardial infarction , stroke, gram-positive shock, gram-negative shock, sepsis, septic shock, hemorrhagic shock, anaphylactic shock, and systemic inflammatory response syndrome.

In some embodiments, the present disclosure provides a therapeutic agent (e.g., an activatable therapeutic agent, or a non-natural activatable therapeutic agent) comprising a release segment (RS) linked directly or indirectly to a biologically active moiety (BM), , wherein RS comprises a peptide substrate having an amino acid sequence susceptible to cleavage by a mammalian protease at the cleavable linkage, the peptide substrate with respect to the sequence set forth in column II or column III (or a subset thereof) of Table A. Includes amino acid sequences having up to 3 amino acid substitutions (or up to 2 amino acid substitutions, or up to 1 amino acid substitution).

In some embodiments, the present disclosure provides a therapeutic agent (e.g., an activatable therapeutic agent, or a non-natural activatable therapeutic agent) comprising a release segment (RS) linked directly or indirectly to a biologically active moiety (BM), , wherein the RS comprises a peptide substrate having an amino acid sequence susceptible to cleavage by a mammalian protease at a cleavable linkage, and the therapeutic agent is configured to be activated in or near a target tissue or cell of a subject;

The target tissue or cell is associated with the reporter sequence in or on or in close proximity thereto, a reporter sequence capable of being cleaved by a mammalian protease at the cleavage sequence;

The peptide substrate comprises an amino acid sequence with up to 3 amino acid substitutions (or up to 2 amino acid substitutions, or up to 1 amino acid substitution) relative to the cleavage sequence of the reporter polypeptide.

In some embodiments of the therapeutic agent, the reporter polypeptide is a coagulation factor, complement component, tubulin, immunoglobulin, apolipoprotein, serum amyloid, insulin, growth factor, fibrinogen, PDZ domain protein, LIM domain protein, c-reactive protein, serum Albumin, versican, collagen, elastin, keratin, kininogen-1, alpha-2-antiplasmin, clustererin, biglycan, alpha-1-antitrypsin, transthyretin, alpha-1-antichymo Trypsin, glucagon, hepcidin, thymosin beta-4, haptoglobin, hemoglobin subunit alpha, vesicle-associated protein 2, alpha-2-HS-glycoprotein, chromogranin-A, vitronectin, hemopexin, epididymis secretory sperm binding protein, secretogranin-2, angiotensinogen, transgelin-2, pancreatic prohormone, neurosecretory protein VGF, ceruloplasmin, PDZ and LIM domain protein 1, multimerin-1, inter- Alpha-trypsin inhibitor heavy chain H2, N-acetylmuramoyl-L-alanine amidase, histone H1.4, adhesion G-protein coupled receptor G6, mannan binding lectin serine protease 2, prothrombin, 1 protein deleted in malignant brain tumors ( deleted in malignant brain tumors 1 protein), desmoglein-3, calcintenin-1, alpha-2-macroglobulin, myosin-9, sodium/potassium transport ATPase subunit gamma, oncoprotein-derived transcript 3 protein, ser Glycine, histidine rich glycoprotein, inter-alpha-trypsin inhibitor heavy chain H5, integrin alpha-IIb, membrane associated progesterone receptor component 1, histone H1.2, rho GDP-dissociation inhibitor 2, zinc-alpha-2-sugar Protein, Talin-1, Secretogranin-1, Neutrophil Defensin 3, Cytochrome P450 2E1, Gastric Inhibitory Polypeptide, Transcription Initiation Factor TFIID Subunit 1, Integral Membrane Protein 2B, Pigmented Epithelial Derived Factor, Voltage-dependent Type N Calcium Channel Subunit alpha-1B, ras GTPase-activating protein nGAP, type I cytoskeleton 17, sulfhydryl oxidase 1, homeobox protein Hox-B2, transcription factor SOX-10, E3 ubiquitin-protein ligase SIAH2, decorin , secreted protein acidic and rich in cysteine (SPARC), laminin gamma 1 chain, vimentin and nidogen-1 (NID1).

In some embodiments of the therapeutic, the reporter polypeptide is versican, type II collagen alpha-1 chain, kininogen-1, complement C4-A, complement C4-B, complement C3, alpha-2-antiplasmin, clu Sterin, biglycan, elastin, fibrinogen alpha chain, alpha-1-antitrypsin, fibrinogen beta chain, type III collagen alpha-1 chain, serum amyloid A-1 protein, transthyretin, apolipoprotein A-I, apolipoprotein A-I isoform 1, alpha-1-antichymotrypsin, glucagon, hepcidin, serum amyloid A-2 protein, thymosin beta-4, haptoglobin, hemoglobin subunit alpha, vesicle-associated protein 2, alpha-2-HS -Glycoprotein, chromogranin-A, vitronectin, hemopexin, epididymal secreted sperm binding protein, direct skin, apolipoprotein C-III, secretogranin-2, angiotensinogen, c-reactive protein, serum Albumin, transgelin-2, pancreatic prohormone, neurosecretory protein VGF, ceruloplasmin, PDZ and LIM domain protein 1, tubulin alpha-4A chain, multimerin-1, inter-alpha-trypsin inhibitor heavy chain H2, apo Lipoprotein C-I, fibrinogen gamma chain, N-acetylmuramoyl-L-alanine amidase, immunoglobulin lambda variable 3-21, histone H1.4, attached G-protein coupled receptor G6, immunoglobulin lambda variable 3-25, immunity Globulin lambda variable 1-51, immunoglobulin lambda variable 1-36, mannan-binding lectin serine protease 2, immunoglobulin kappa variable 3-20, immunoglobulin kappa variable 2-30, insulin-like growth factor II, apolipoprotein A-II , probable nonfunctional immunoglobulin kappa variable 2D-24, prothrombin, coagulation factor IX, apolipoprotein L1, 1 protein deleted in malignant brain tumor, desmoglein-3, calcintenin-1, immunoglobulin lambda constant 3, Complement C5, alpha-2-macroglobulin, myosin-9, sodium/potassium transport ATPase subunit gamma, immunoglobulin kappa variable 2-28, oncoprotein-derived transcript 3 protein, serglycin, coagulation factor XII, coagulation factor XIII A chain, insulin, histidine rich glycoprotein, immunoglobulin kappa variable 3-11, immunoglobulin kappa variable 1-39, collagen alpha-1(I) chain, inter-alpha-trypsin inhibitor heavy chain H5, potential transforming growth factor beta binding protein 2, integrin alpha-IIb, membrane-associated progesterone receptor component 1, immunoglobulin lambda variable 6-57, immunoglobulin kappa variable 3-15, complement C1r subcomponent-like protein, histone H1.2, Rho GDP-dissociation inhibitor 2, potential transforming growth factor beta binding protein 4, collagen alpha-1 (XVIII) chain, immunoglobulin lambda variable 2-18, zinc-alpha-2-glycoprotein, talin-1, secretogranin-1, neutrophil defensin 3, Cytochrome P450 2E1, Gastric Inhibitory Polypeptide, Immunoglobulin Heavy Chain Variable 3-15, Immunoglobulin Lambda Variable 2-11, Transcription Initiation Factor TFIID Subunit 1, Collagen Alpha-1 (VII) Chain, Integral Membrane Protein 2B, Pigmented Epithelial Derived Factor , voltage-dependent N-type calcium channel subunit alpha-1B, immunoglobulin lambda variable 3-27, ras GTPase-activating protein nGAP, keratin, type I cytoskeleton 17, tubulin beta chain, sulfhydryl oxidase 1, immunoglobulin Kappa variable 4-1, complement C1r subcomponent, homeobox protein Hox-B2, transcription factor SOX-10, E3 ubiquitin-protein ligase SIAH2, decorin, SPARC, type I collagen alpha-1 chain, type IV collagen alpha -1 chain, laminin gamma 1 chain, vimentin, type III collagen, type IV collagen alpha-3 chain, type VII collagen alpha-1 chain, type VI collagen alpha-1 chain, type V collagen alpha-1 chain, nidogen -1 and type VI collagen alpha-3 chains.

In some embodiments of the therapeutic agent, the cleavage sequence of the reporter polypeptide is a cleavage sequence set forth in column II or column III of Table A (or a subset thereof). In some embodiments, the cleavage sequence does not include a methionine residue immediately N-terminal to a cleavable linkage (contained therein) if methionine is the first residue N-terminal to the reporter polypeptide. In some embodiments, the target tissue or cell is characterized by an increased amount or activity of a mammalian protease proximal to the target tissue or cell compared to a non-target tissue or cell of the subject. In some embodiments, the mammalian protease is produced in a target tissue or cell. In some embodiments, the peptide substrate is an amino acid sequence having up to 3 amino acid substitutions, or up to 2 amino acid substitutions, or up to 1 amino acid substitution relative to a sequence set forth in column II or III (or a subset thereof) of Table A. includes In some embodiments, the peptide substrate comprises an amino acid sequence with up to 3 amino acid substitutions relative to a sequence set forth in column II or III of Table A (or a subset thereof). In some embodiments, the cleavable linkage is not immediately C-terminal to the methionine residue.

In some embodiments of the therapeutic agent, the peptide substrate contains 6 to 25 or 6 to 20 amino acid residues. In some embodiments of the therapeutic agent, the peptide substrate contains between 6 and 25 amino acid residues. In some embodiments of the therapeutic agent, the peptide substrate contains 6 to 20 amino acid residues. In some embodiments, the peptide substrate contains 7 to 12 amino acid residues. In some embodiments, the peptide substrate comprises an amino acid sequence with up to two amino acid substitutions relative to a sequence set forth in column II or column III of Table A (or a subset thereof). In some embodiments, the peptide substrate comprises an amino acid sequence with up to one amino acid substitution relative to a sequence set forth in column II or III of Table A (or a subset thereof). In some embodiments, none of the up to 3 amino acid substitutions, or up to 2 amino acid substitutions, or up to 1 amino acid substitutions is a corresponding truncation of the corresponding sequence set forth in column II or III (or a subset thereof) of Table A. It is not in a position corresponding to an amino acid residue immediately adjacent to a likely linkage. In some embodiments, the peptide substrate comprises an amino acid sequence identical to a sequence set forth in column II or column III of Table A (or a subset thereof). In some embodiments, the peptide substrate does not include a methionine residue immediately N-terminal to the cleavable linkage contained therein). In some embodiments , the peptide substrate is #279, #280, #282, #283, #298, #299, #302, #303, #305, #307, #308, #349, Does not contain an amino acid sequence selected from the group consisting of #396, #397, #416, #417, #418, #458, #459, #460, #466, #481 and #482 (or any combination thereof) . In some embodiments, the peptide substrate comprises two or three sequences set forth in column II or column III of Table A (or a subset thereof). In some embodiments, when the peptide substrate comprises two sequences set forth in column II or III (or a subset thereof) of Table A , the two sequences partially overlap each other. In some embodiments, when the peptide substrate comprises two sequences set forth in column II or column III of Table A (or a subset thereof), the two sequences do not overlap with each other. In some embodiments, where the peptide substrate comprises three sequences set forth in column II or III (or a subset thereof) of Table A , two or all of the three sequences do not overlap with each other. In some embodiments, where the peptide substrate comprises three sequences set forth in column II or III (or a subset thereof) of Table A , one of the three sequences is another sequence or the other two of the three sequences. partially overlaps with the sequence. In some embodiments, where the peptide substrate comprises three sequences set forth in column II or III (or a subset thereof) of Table A , two of the three sequences partially overlap each other. In some embodiments, where the peptide substrate comprises three sequences set forth in column II or III (or a subset thereof) of Table A , two of each of the three sequences partially overlap one another. In some embodiments, when the peptide substrate comprises three sequences set forth in column II or III (or a subset thereof) of Table A , all three sequences partially overlap each other. In some embodiments, a peptide substrate susceptible to cleavage by a mammalian protease is susceptible to cleavage by a plurality of mammalian proteases, including mammalian proteases. In some embodiments, the peptide substrate susceptible to cleavage by a plurality of mammalian proteases has up to 3 amino acid substitutions, or up to 2 amino acid substitutions, or up to 1 amino acid substitution relative to the sequence shown in Table 1(j) . In some embodiments, the peptide substrate susceptible to cleavage by multiple mammalian proteases has up to three amino acid substitutions relative to the sequence shown in Table 1(j) . In some embodiments, the peptide substrate susceptible to cleavage by multiple mammalian proteases has up to two amino acid substitutions relative to the sequence shown in Table 1(j) . In some embodiments, the peptide substrate susceptible to cleavage by multiple mammalian proteases has at most one amino acid substitution relative to the sequence shown in Table 1(j) . In some embodiments, none of up to three amino acid substitutions, or up to two amino acid substitutions, or up to one amino acid substitution are in an amino acid residue immediately adjacent to the corresponding scissile bond of the corresponding sequence set forth in Table 1(j). not in the corresponding position. In some embodiments, the peptide substrate susceptible to cleavage by a plurality of mammalian proteases comprises a sequence shown in Table 1(j) .

In some embodiments of the therapeutic, the release segment (RS) can be cleaved upon proximity to a target tissue or cell, wherein the target tissue or cell produces a mammalian protease in which the RS is a peptide substrate. In some embodiments, the mammalian protease for cleavage of the release segment (RS) is a serine protease, cysteine protease, aspartate protease, threonine protease or metalloproteinase. In some embodiments, the mammalian protease for cleavage of the release segment (RS) is Disintegrin and Metalloproteinase Domain Containing Protein 10 (ADAM10), Disintegrin and Metalloproteinase Domain Containing Protein 12 (ADAM12), disintegrin and metalloproteinase domain-containing protein 15 (ADAM15), disintegrin and metalloproteinase domain-containing protein 17 (ADAM17), disintegrin and metalloproteinase domain-containing protein 9 (ADAM9), thrombos Disintegrin and metalloproteinase (ADAMTS5) with fondin motif 5, cathepsin B, cathepsin D, cathepsin E, cathepsin K, cathepsin L, cathepsin S, fibroblast activation protein alpha, hepsin, kali Crane-2, kallikrein-4, kallikrein-3, prostate specific antigen (PSA), kallikrein-13, legumain, matrix metallopeptidase 1 (MMP-1), matrix metallopeptidase 10 (MMP-10), Matrix Metallopeptidase 11 (MMP-11), Matrix Metallopeptidase 12 (MMP-12), Matrix Metallopeptidase 13 (MMP-13), Matrix Metallopeptidase tidase 14 (MMP-14), matrix metallopeptidase 16 (MMP-16), matrix metallopeptidase 2 (MMP-2), matrix metallopeptidase 3 (MMP-3), matrix metal Lopeptidase 7 (MMP-7), Matrix Metallopeptidase 8 (MMP-8), Matrix Metallopeptidase 9 (MMP-9), Matrix Metallopeptidase 4 (MMP-4), Matrix metallopeptidase 5 (MMP-5), matrix metallopeptidase 6 (MMP-6), matrix metallopeptidase 15 (MMP-15), neutrophil elastase, protease activated receptor 2 (PAR2) ), plasmin, prostacin, PSMA-FOLH1, membrane type serine protease 1 (MT-SP1), matriptase and u-plasminogen. In some embodiments, the mammalian protease for cleavage of the release segment (RS) is matrix metallopeptidase 1 (MMP1), matrix metallopeptidase 2 (MMP2), matrix metallopeptidase 7 (MMP7) , matrix metallopeptidase 9 (MMP9), matrix metallopeptidase 11 (MMP11), matrix metallopeptidase 14 (MMP14), urokinase-type plasminogen activator (uPA), legumain and It is selected from the group consisting of matriptase.

In some embodiments of the therapeutic agent, the therapeutic agent further comprises a masking moiety (MM) linked directly or indirectly to the emitting segment (RS). In some embodiments, the therapeutic agent in its uncleaved state has the N-terminus to C-terminus structural arrangement of BM-RS-MM or MM-RS-BM. In some embodiments of the therapeutic agent, upon cleavage of the releasing segment (RS), the masking moiety (MM) is released from the therapeutic agent. In some embodiments, the masking moiety (MM) comprises an extended recombinant polypeptide (XTEN). In some embodiments, an XTEN is characterized by: (i) comprises at least 100 amino acids; (ii) at least 90% of the amino acid residues are selected from glycine (G), alanine (A), serine (S), threonine (T), glutamate (E) and proline (P); (iii) at least four different types of amino acids selected from G, A, S, T, E and P. In some embodiments, the extended recombinant polypeptide (XTEN) is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% of the sequence shown in Tables 2b-2c. %, or amino acid sequences that have 100% sequence identity. In some embodiments, the masking moiety (MM), when linked to the therapeutic agent, interferes with the interaction of the biologically active moiety (BM) to the target tissue or cell, such that the therapeutic agent, when in an uncleaved state, does not bind to the target tissue or cell. The dissociation constant (K _d ) of the BM of the therapeutic and the target cell marker carried by the cell is greater compared to the dissociation constant (K _d ) of the target cell marker and the corresponding biologically active moiety. In some embodiments, the therapeutic agent results in a wider therapeutic window in the delivery of the BM to the target tissue or cell compared to the corresponding biologically active moiety. In some embodiments, the therapeutic agent has a longer elimination half-life compared to the corresponding biologically active moiety. In some embodiments, the therapeutic agent is less immunogenic compared to the corresponding biologically active moiety. In some embodiments, immunogenicity is determined by measuring the production of IgG antibodies that selectively bind to biologically active moieties after administration of similar doses to a subject. In some embodiments, the therapeutic agent has a higher apparent molecular weight factor under physiological conditions compared to the corresponding biologically active moiety.

In some embodiments of the therapeutic agent, the releasing segment (RS) is a first emitting segment (RS1), wherein the cleavable bond is the first cleavable bond, and the therapeutic agent is directly or indirectly to the biologically active moiety (BM). and further comprising a linked second release segment (RS2), wherein RS2 comprises a second peptide substrate or comprises cleavage by a mammalian protease at a second cleavable linkage. In some embodiments, the mammalian protease for cleavage of RS2 is the same mammalian protease for cleavage of RS1. In some embodiments, the mammalian protease for cleavage of RS2 is different from the mammalian protease for cleavage of RS1. In some embodiments, RS2 has the same amino acid sequence as RS1. In some embodiments, RS2 has a different amino acid sequence than RS1. In some embodiments, each of RS1 and RS2 is disintegrin and metalloproteinase domain containing protein 10 (ADAM10), disintegrin and metalloproteinase domain containing protein 12 (ADAM12), disintegrin and metalloproteinase protein 15 containing domain (ADAM15), disintegrin and metalloproteinase domain containing protein 17 (ADAM17), disintegrin and metalloproteinase domain containing protein 9 (ADAM9), disintegrin with thrombospondin motif 5 and Metalloproteinase (ADAMTS5), cathepsin B, cathepsin D, cathepsin E, cathepsin K, cathepsin L, cathepsin S, fibroblast activation protein alpha, hepsin, kallikrein-2, kallikrein-4 , kallikrein-3, prostate specific antigen (PSA), kallikrein-13, legumain, matrix metallopeptidase 1 (MMP-1), matrix metallopeptidase 10 (MMP-10), matrix Metallopeptidase 11 (MMP-11), Matrix Metallopeptidase 12 (MMP-12), Matrix Metallopeptidase 13 (MMP-13), Matrix Metallopeptidase 14 (MMP-14) , matrix metallopeptidase 16 (MMP-16), matrix metallopeptidase 2 (MMP-2), matrix metallopeptidase 3 (MMP-3), matrix metallopeptidase 7 (MMP- 7), matrix metallopeptidase 8 (MMP-8), matrix metallopeptidase 9 (MMP-9), matrix metallopeptidase 4 (MMP-4), matrix metallopeptidase 5 ( MMP-5), matrix metallopeptidase 6 (MMP-6), matrix metallopeptidase 15 (MMP-15), neutrophil elastase, protease activated receptor 2 (PAR2), plasmin, prostasin , PSMA-FOLH1, membrane type serine protease 1 (MT-SP1), matriptase and u-plasminogen. In some embodiments, each of RS1 and RS2 is matrix metallopeptidase 1 (MMP1), matrix metallopeptidase 2 (MMP2), matrix metallopeptidase 7 (MMP7), matrix metallopeptidase 9 (MMP9), matrix metallopeptidase 11 (MMP11), matrix metallopeptidase 14 (MMP14), urokinase-type plasminogen activator (uPA), legumain and matriptase. Includes peptide substrates for mammalian proteases. In some embodiments, the second cleavable linkage is not immediately C-terminal to the methionine residue.

In some embodiments of the therapeutic agent, the second peptide substrate contains 6 to 25 or 6 to 20 amino acid residues. In some embodiments of the therapeutic agent, the second peptide substrate contains between 6 and 25 amino acid residues. In some embodiments of the therapeutic agent, the second peptide substrate contains 6 to 20 amino acid residues. In some embodiments, the second peptide substrate contains 7 to 12 amino acid residues. In some embodiments, the second peptide substrate has up to 3 amino acid substitutions, or up to 2 amino acid substitutions, or up to 1 amino acid substitution relative to a sequence set forth in column II or III (or a subset thereof) of Table A. contains an amino acid sequence. In some embodiments, the second peptide substrate comprises an amino acid sequence with up to three amino acid substitutions relative to a sequence set forth in column II or III of Table A (or a subset thereof). In some embodiments, the second peptide substrate comprises an amino acid sequence with up to two amino acid substitutions relative to a sequence set forth in column II or column III of Table A (or a subset thereof). In some embodiments, the second peptide substrate comprises an amino acid sequence with up to one amino acid substitution to a sequence set forth in column II or III of Table A (or a subset thereof). In some embodiments, none of up to three amino acid substitutions, or up to two amino acid substitutions, or up to one amino acid substitution (of the second peptide substrate) are set forth in column II or III (or a subset thereof) of Table A. It is not positioned to correspond to an amino acid residue immediately adjacent to the corresponding cleavable linkage of the corresponding sequence. In some embodiments, the second peptide substrate comprises an amino acid sequence identical to a sequence set forth in column II or column III of Table A (or a subset thereof). In some embodiments, the second peptide substrate does not include a methionine residue immediately N-terminal to the cleavable bond (contained therein). In some embodiments, the second peptide substrate is #279, #280, #282, #283, #298, #299, #302, #303, #305, #307, #308, # of column II of Table A. 349, #396, #397, #416, #417, #418, #458, #459, #460, #466, #481 and #482 (or any combination thereof) comprising an amino acid sequence selected from the group consisting of: I never do that. In some embodiments, the second peptide substrate comprises two or three sequences set forth in column II or column III of Table A (or a subset thereof). In some embodiments, when the second peptide substrate comprises two sequences set forth in column II or III (or a subset thereof) of Table A , the two sequences (of the second peptide substrate) partially overlap each other. . In some embodiments, when the second peptide substrate comprises two sequences set forth in column II or III (or a subset thereof) of Table A , the two sequences (of the second peptide substrate) do not overlap with each other. In some embodiments, where the second peptide substrate comprises three sequences set forth in column II or III (or a subset thereof) of Table A , two or all of the three sequences (of the second peptide substrate) do not overlap each other In some embodiments, where the second peptide substrate comprises three sequences set forth in column II or III (or a subset thereof) of Table A , one of the three sequences (of the second peptide substrate) is another sequence. or partially overlapping sequences of both of the other three sequences (of the second peptide substrate). In some embodiments, where the second peptide substrate comprises three sequences set forth in column II or III (or a subset thereof) of Table A , two of the three sequences (of the second peptide substrate) are partial to each other. overlapped with In some embodiments, where the second peptide substrate comprises three sequences set forth in column II or III (or a subset thereof) of Table A , then two of each of the three sequences (of the second peptide substrate) are mutually exclusive. partially overlapping. In some embodiments, when the second peptide substrate comprises three sequences set forth in column II or III (or a subset thereof) of Table A , all three sequences (of the second peptide substrate) partially overlap each other. do. In some embodiments, the second peptide substrate susceptible to cleavage by a mammalian protease is susceptible to cleavage by a plurality of mammalian proteases, including mammalian proteases. In some embodiments, the second peptide substrate susceptible to cleavage by the plurality of mammalian proteases has up to 3 amino acid substitutions, or up to 2 amino acid substitutions, or up to 1 amino acid substitution relative to the sequence shown in Table 1(j). have In some embodiments, the second peptide substrate susceptible to cleavage by a plurality of mammalian proteases has up to three amino acid substitutions relative to the sequence shown in Table 1(j) . In some embodiments, the second peptide substrate susceptible to cleavage by the plurality of mammalian proteases has up to two amino acid substitutions relative to the sequence shown in Table 1(j) . In some embodiments, the second peptide substrate susceptible to cleavage by the plurality of mammalian proteases has at most one amino acid substitution relative to the sequence shown in Table 1(j) . In some embodiments, none of up to 3 amino acid substitutions, or up to 2 amino acid substitutions, or up to 1 amino acid substitutions (of the second peptide substrate) is the corresponding cleavage-prone of the corresponding sequence shown in Table 1(j). It is not in a position corresponding to the amino acid residue immediately adjacent to the bond. In some embodiments, the second peptide substrate susceptible to cleavage by a plurality of mammalian proteases comprises a sequence shown in Table 1(j) .

In some embodiments of the therapeutic, the second release segment (RS2) can be cleaved upon proximity to a target tissue or cell, wherein the target tissue or cell produces a mammalian protease for which RS2 is a peptide substrate. This includes oncogenic proteases and oncogenic proteases. In some embodiments, the mammalian protease for cleavage of the second release segment (RS2) is a serine protease, cysteine protease, aspartate protease, threonine protease or metalloproteinase. In some embodiments, the mammalian protease for cleavage of the release segment (RS) is Disintegrin and Metalloproteinase Domain Containing Protein 10 (ADAM10), Disintegrin and Metalloproteinase Domain Containing Protein 12 (ADAM12), disintegrin and metalloproteinase domain-containing protein 15 (ADAM15), disintegrin and metalloproteinase domain-containing protein 17 (ADAM17), disintegrin and metalloproteinase domain-containing protein 9 (ADAM9), thrombos Disintegrin and metalloproteinase (ADAMTS5) with fondin motif 5, cathepsin B, cathepsin D, cathepsin E, cathepsin K, cathepsin L, cathepsin S, fibroblast activation protein alpha, hepsin, kali Crane-2, kallikrein-4, kallikrein-3, prostate specific antigen (PSA), kallikrein-13, legumain, matrix metallopeptidase 1 (MMP-1), matrix metallopeptidase 10 (MMP-10), Matrix Metallopeptidase 11 (MMP-11), Matrix Metallopeptidase 12 (MMP-12), Matrix Metallopeptidase 13 (MMP-13), Matrix Metallopeptidase tidase 14 (MMP-14), matrix metallopeptidase 16 (MMP-16), matrix metallopeptidase 2 (MMP-2), matrix metallopeptidase 3 (MMP-3), matrix metal Lopeptidase 7 (MMP-7), Matrix Metallopeptidase 8 (MMP-8), Matrix Metallopeptidase 9 (MMP-9), Matrix Metallopeptidase 4 (MMP-4), Matrix metallopeptidase 5 (MMP-5), matrix metallopeptidase 6 (MMP-6), matrix metallopeptidase 15 (MMP-15), neutrophil elastase, protease activated receptor 2 (PAR2) ), plasmin, prostacin, PSMA-FOLH1, membrane type serine protease 1 (MT-SP1), matriptase and u-plasminogen. In some embodiments, the mammalian protease for cleavage of the second release segment (RS2) is matrix metallopeptidase 1 (MMP1), matrix metallopeptidase 2 (MMP2), matrix metallopeptidase 7 ( MMP7), matrix metallopeptidase 9 (MMP9), matrix metallopeptidase 11 (MMP11), matrix metallopeptidase 14 (MMP14), urokinase-type plasminogen activator (uPA), leguma It is selected from the group consisting of phosphorus and matriptase.

In some embodiments of the therapeutic agent, the masking moiety (MM) is a first masking moiety (MM1) and the therapeutic agent further comprises a second masking moiety (MM2) connected directly or indirectly to the second emitting segment (RS2). include In some embodiments, the therapeutic agent in the uncut state is MM1-RS1-BM-RS2-MM2, MM1-RS2-BM-RS1-MM2, MM2-RS1-BM-RS2-MM1, or MM2-RS2-BM-RS1- It has a structural arrangement from the N-terminus to the C-terminus of MM1. In some embodiments of the therapeutic agent, upon cleavage of the second releasing segment (RS2), the second masking moiety (MM2) is released from the therapeutic agent. In some embodiments, the second masking moiety (MM2) comprises a second extended recombinant polypeptide (XTEN2). In some embodiments, XTEN2 is characterized by: (i) comprises at least 100 amino acids; (ii) at least 90% of the amino acid residues are selected from glycine (G), alanine (A), serine (S), threonine (T), glutamate (E) and proline (P); (iii) at least four different types of amino acids selected from G, A, S, T, E and P. In some embodiments, XTEN2 is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% of a sequence selected from the group of sequences set forth in Tables 2b-2c. , or an amino acid sequence with 100% sequence identity. In some embodiments, both the first masking moiety (MM1) and the second masking moiety (MM2), when linked in a therapeutic agent, interfere with the interaction of the biologically active moiety (BM) with the target tissue or cell, As a result, when the therapeutic agent is in its uncleaved state, the dissociation constant (K _d ) of the target cell marker carried by the target tissue or cell and the BM of the therapeutic agent is greater compared to the dissociation constant (K _d ) of the corresponding biologically active moiety. big. In some embodiments, a therapeutic agent in which the biologically active moiety (BM) is directly or indirectly linked to one or both of the first masking moiety (MM1) and the second masking moiety (MM2) comprises a corresponding biologically active moiety and Comparatively, this results in a wider therapeutic window in the delivery of BM to target tissues or cells. In some embodiments, a therapeutic agent in which the biologically active moiety (BM) is directly or indirectly linked to one or both of the first masking moiety (MM1) and the second masking moiety (MM2) comprises a corresponding biologically active moiety and have a relatively longer elimination half-life. In some embodiments, a therapeutic agent in which the biologically active moiety (BM) is directly or indirectly linked to one or both of the first masking moiety (MM1) and the second masking moiety (MM2) comprises a corresponding biologically active moiety and comparatively less immunogenic. In some embodiments of the therapeutic agent, immunogenicity is determined by measuring the production of IgG antibodies that selectively bind to biologically active moieties following administration of similar doses to a subject. In some embodiments, a therapeutic agent in which the biologically active moiety (BM) is directly or indirectly linked to one or both of the first masking moiety (MM1) and the second masking moiety (MM2) comprises a corresponding biologically active moiety and comparatively have a larger apparent molecular weight factor under physiological conditions. In some embodiments, the therapeutic agent comprises a fusion polypeptide or conjugate.

In some embodiments of the therapeutic agent, the biologically active moiety (BM) comprises a biologically active peptide (BP). In some embodiments, the BP comprises an antibody, cytokine, cellular receptor or fragment thereof.

In some embodiments, the therapeutic agent comprises a recombinant polypeptide. In some embodiments, the recombinant polypeptide comprises a biologically active peptide (BP) and a release segment (RS). In some embodiments, the recombinant polypeptide comprises a biologically active peptide (BP), a releasing segment (RS) and a masking moiety (MM). In some embodiments, the recombinant polypeptide in its untruncated state has the N-terminus to C-terminus structural arrangement of BP-RS-MM or MM-RS-BP. In some embodiments, the recombinant polypeptide comprises a biologically active peptide (BP), a first emitting segment (RS1) and a second emitting segment (RS2). In some embodiments, the recombinant polypeptide comprises a biologically active peptide (BP), a first emitting segment (RS1), a second emitting segment (RS2), a first masking moiety (MM1) and a second masking moiety (MM2) do. In some embodiments, the recombinant polypeptide in the uncleaved state is MM1-RS1-BP-RS2-MM2, MM1-RS2-BP-RS1-MM2, MM2-RS1-BP-RS2-MM1, or MM2-RS2-BP-RS1 -It has a structural arrangement from the N-terminus to the C-terminus of MM1. In some embodiments, the recombinant polypeptide comprises a biologically active peptide (BP), a first emissive segment (RS1), a second emissive segment (RS2), a first extended recombinant polypeptide (XTEN1) and a second extended recombinant polypeptide (XTEN2). includes In some embodiments, the recombinant polypeptide in its uncut state is XTEN1-RS1-BP-RS2-XTEN2, XTEN1-RS2-BP-RS1-XTEN2, XTEN2-RS1-BP-RS2-XTEN1, or XTEN2-RS2-BP-RS1 -It has a structural arrangement from the N-terminus to the C-terminus of XTEN1.

In some embodiments of the therapeutic agent, the biologically active polypeptide (BP) comprises a binding moiety that has binding affinity for a target cell marker on a target tissue or cell. In some embodiments, the target cell marker is an effector cell antigen expressed on the surface of an effector cell. In some embodiments, the binding moiety is an antibody. In some embodiments, the binding moiety is an antibody selected from the group consisting of Fv, Fab, Fab', Fab'-SH, nanobodies (also known as single domain antibodies or V _HH ), linear antibodies, and single chain variable fragments (scFv). . In some embodiments, the binding moiety is a first binding moiety, wherein the target cell marker is a first target cell marker, and the biologically active polypeptide (BP) is a second binding moiety linked directly or indirectly to the first binding moiety. Further comprising, wherein the second binding moiety has binding affinity for a second target cell marker on the target tissue or cell. In some embodiments, the second target cell marker is a marker on tumor cells or cancer cells. In some embodiments, the second binding moiety is an antibody. In some embodiments, the second binding moiety is selected from the group consisting of Fv, Fab, Fab', Fab'-SH, nanobodies (also known as single domain antibodies or V _HH ), linear antibodies and single chain variable fragments (scFv). is an antibody

Certain aspects of the present disclosure provide an isolated nucleic acid comprising: (a) a polynucleotide encoding a recombinant polypeptide described herein; or (b) the reverse complement of the polynucleotide of (a).

Certain aspects of the present disclosure provide an expression vector, the expression vector comprising a polynucleotide sequence as described herein and a recombination control sequence operably linked to the polynucleotide sequence.

Certain aspects of the present disclosure provide an isolated host cell, wherein the isolated host cell comprises an expression vector as described herein. In some embodiments, the host cell is prokaryotic. In some embodiments, the host cell is an E. coli or mammalian cell. In some embodiments, the host cell is E. coli. In some embodiments, the host cell is a mammalian cell.

Some aspects of the present disclosure provide a pharmaceutical composition comprising a therapeutic agent as described herein and one or more pharmaceutically suitable excipients. In some embodiments, the pharmaceutical composition is formulated for oral, intradermal, subcutaneous, intravenous, intraarterial, intraperitoneal, intraperitoneal, intrathecal or intramuscular administration. In some embodiments, the pharmaceutical composition is in liquid or frozen form. In some embodiments, the pharmaceutical composition is presented as a pre-filled syringe for single injection. In some embodiments, the pharmaceutical composition is formulated as a lyophilized powder that is reconstituted prior to administration.

Some aspects of the present disclosure provide kits, which include a pharmaceutical composition as described herein, a container, and a label or package insert on or associated with the container.

In certain embodiments, the present disclosure provides methods of making a therapeutic agent (eg, an activatable therapeutic agent, or a non-natural activatable therapeutic agent) as provided herein.

In certain embodiments, the present disclosure provides methods of making a therapeutic agent (eg, an activatable therapeutic agent, or a non-natural activatable therapeutic agent), the method comprising:

(a) culturing a host cell comprising a nucleic acid construct encoding the recombinant polypeptide under conditions sufficient to allow expression of the recombinant polypeptide in the host cell, wherein the recombinant polypeptide comprises a biologically active polypeptide (BP), a release segment (RS) and a masking moiety (MM),

The RS contains a peptide substrate susceptible to cleavage by mammalian proteases at its cleavable linkage, wherein the peptide substrate has up to three or two amino acids to the sequence shown in column II or III (or a subset thereof) of Table A. comprises an amino acid sequence with amino acid substitutions (or at most one amino acid substitution);

The recombinant polypeptide has a structural arrangement from the N-terminus to the C-terminus of BP-RS-MM or MM-RS-BP; and

(b) recovering a therapeutic agent (eg, an activatable therapeutic agent, or a non-naturally occurring activatable therapeutic agent) comprising the recombinant polypeptide.

In some embodiments of the method of making a therapeutic agent, the peptide substrate susceptible to cleavage by a mammalian protease is susceptible to cleavage by a plurality of mammalian proteases, including mammalian proteases. In some embodiments, the peptide substrate susceptible to cleavage by a plurality of mammalian proteases has up to 3 amino acid substitutions, or up to 2 amino acid substitutions, or up to 1 amino acid substitution relative to the sequence shown in Table 1(j) . In some embodiments, the peptide substrate susceptible to cleavage by a plurality of mammalian proteases comprises a sequence shown in Table 1(j) . In some embodiments, the peptide substrate does not include SEQ ID NO: 1 . In some embodiments, the peptide substrate does not include SEQ ID NO:2 . In some embodiments, the peptide substrate does not include SEQ ID NO:3 . In some embodiments, the peptide substrate does not include SEQ ID NO:4 . In some embodiments, the peptide substrate does not include SEQ ID NO:5 . In some embodiments, the peptide substrate does not include SEQ ID NO:6 . In some embodiments, the peptide substrate does not include SEQ ID NO:7 . In some embodiments, the peptide substrate does not include SEQ ID NO:8 . In some embodiments, the masking moiety (MM) comprises an extended recombinant polypeptide (XTEN).

In some embodiments of the method of making a therapeutic agent, the emitting segment (RS) is a first emitting segment (RS1), wherein the peptide substrate is a first peptide substrate, the cleavable bond is a first cleavable bond, and the masking Moiety (MM) is a first masking moiety (MM1) and the recombinant polypeptide further comprises a second emissive segment (RS2) and a second masking moiety (MM2), wherein RS2 is a second cleavable bond a second peptide substrate susceptible to cleavage by mammalian proteases in , wherein the second peptide substrate comprises at most three amino acid substitutions relative to the sequence set forth in column II or column III (or a subset thereof) of Table A , or at most comprises an amino acid sequence with two amino acid substitutions, or at most one amino acid substitution; The recombinant polypeptide is C- from the N-terminus of MM1-RS1-BP-RS2-MM2, MM1-RS2-BP-RS1-MM2, MM2-RS1-BP-RS2-MM1, or MM2-RS2-BP-RS1-MM1. It has a structural arrangement all the way to the end.

In some embodiments of the method of making a therapeutic agent, the second peptide substrate susceptible to cleavage by a mammalian protease is susceptible to cleavage by a plurality of mammalian proteases, including mammalian proteases. In some embodiments, the second peptide substrate susceptible to cleavage by the plurality of mammalian proteases has up to 3 amino acid substitutions, or up to 2 amino acid substitutions, or up to 1 amino acid substitution relative to the sequence shown in Table 1(j). have In some embodiments, the second peptide substrate susceptible to cleavage by a plurality of mammalian proteases comprises a sequence shown in Table 1(j) . In some embodiments, the second peptide substrate does not include SEQ ID NO:1 . In some embodiments, the second peptide substrate does not include SEQ ID NO:2 . In some embodiments, the second peptide substrate does not include SEQ ID NO:3 . In some embodiments, the second peptide substrate does not include SEQ ID NO:4 . In some embodiments, the second peptide substrate does not include SEQ ID NO:5 . In some embodiments, the second peptide substrate does not include SEQ ID NO:6 . In some embodiments, the second peptide substrate does not include SEQ ID NO:7 . In some embodiments, the second peptide substrate does not include SEQ ID NO:8 . In some embodiments, one of the first masking moiety (MM1) and the second masking moiety (MM2) comprises an extended recombinant polypeptide (XTEN). In some embodiments, the extended recombinant polypeptide (XTEN) is characterized by: (i) comprises at least 100 amino acids; (ii) at least 90% of the amino acid residues are selected from glycine (G), alanine (A), serine (S), threonine (T), glutamate (E) and proline (P); (iii) at least four different types of amino acids selected from G, A, S, T, E and P. In some embodiments, the extended recombinant polypeptide (XTEN) is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% of a sequence selected from the group set forth in Tables 2b-2c. amino acid sequences that have %, 99%, or 100% sequence identity. In some embodiments, the extended recombinant polypeptide (XTEN) is a first extended recombinant polypeptide (XTEN1), wherein the other of the first masking moiety (MM1) and the second masking moiety (MM2) is a second extended recombinant polypeptide (XTEN1). Recombinant polypeptide (XTEN2). In some embodiments, the second extended recombinant polypeptide (XTEN2) is characterized by: (i) comprises at least 100 amino acids; (ii) at least 90% of the amino acid residues are selected from glycine (G), alanine (A), serine (S), threonine (T), glutamate (E) and proline (P); (iii) at least four different types of amino acids selected from G, A, S, T, E and P. In some embodiments, each of XTEN1 and XTEN2 is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% of a sequence selected from the group of sequences set forth in Tables 2b-2c. , amino acid sequences that have 99%, or 100% sequence identity.

In some embodiments of the method of making a therapeutic agent, the masking moiety (MM), when linked to the recombinant polypeptide, interferes with the interaction of the BP with the target tissue or cell, such that when the recombinant polypeptide is in an uncleaved state, the target The dissociation constant (K _d ) of the target cell marker carried by the tissue or cell and the BP of the recombinant polypeptide is greater compared to the dissociation constant (K _d ) of the corresponding biologically active peptide measured in an in vitro assay at equivalent molar concentrations . In some embodiments, both the first masking moiety (MM1) and the second masking moiety (MM2), when linked in the recombinant polypeptide, interfere with the interaction of the BP with the target tissue or cell, resulting in the recombinant polypeptide being non- The dissociation constant (K d ) of the BP of the target cell marker and the recombinant polypeptide carried by the target tissue or cell when in the cleaved state is the dissociation constant (K _d ) of the corresponding biologically active peptide determined in an in vitro assay at equimolar concentrations. _d ), which is larger. In some embodiments, the in vitro assay is a cell membrane integrity assay, a mixed cell culture assay, a cell-based competitive binding assay, a FACS-based propidium iodide assay, a trypan blue influx assay, a photometric enzyme release assay, a radiometric 51Cr release assay, a fluorescence assay. Assays Europium release assay, CalceinAM release assay, Photometric MTT assay, XTT assay, WST-1 assay, Alamar blue assay, Radiometric assay 3H-Thd incorporation assay, Clonogenic assay to measure cell division activity, Mitochondrial transmembrane a fluorescence assay that measures a gradient rhodamine 123 assay, a FACS-based apoptosis assay monitored by phosphatidylserine exposure, an ELISA-based TUNEL test assay, a sandwich ELISA, a caspase activity assay, a cell-based LDH release assay and a cell morphology assay, or any of these selected from any combination. In some embodiments, the activatable therapeutic agent is an activatable therapeutic agent as described herein or a non-naturally occurring activatable therapeutic agent.

Additional aspects and advantages of the present disclosure will become readily apparent to those skilled in the art from the following detailed description for practicing the invention, in which only exemplary embodiments of the present disclosure are shown and described. As should be understood, the present disclosure is capable of other and different embodiments, all of its several details being capable of being modified in various obvious respects without departing from this disclosure. Accordingly, the drawings and description are to be regarded as illustrative in nature and not limiting.

included as reference

All publications, patents and patent applications mentioned in this specification are herein incorporated by reference to the same extent as if each individual publication, patent or patent application was specifically and individually indicated to be incorporated by reference. In the event that publications and patents or patent applications incorporated by reference conflict with the disclosure contained herein, this specification is intended to supersede and/or take precedence over any such conflicting material.

The novel features of the invention are pointed out with particularity in the appended claims. A better understanding of the features and advantages of the present invention may be obtained by reference to the following detailed description of the invention, which describes illustrative embodiments in which the principles of the present invention are employed and the accompanying drawings (also "Figures" herein). will lose
1 illustrates the nomenclature of peptide biomarker sequences in a reporter polypeptide (eg, a protein in or adjacent to a target tissue or cell from which the biomarker sequence is generated) (eg, any of those set forth in Table A ). Exemplary reporter polypeptide sequences include two cleavage sequences, a first cleavage sequence and a second cleavage sequence (eg, any of those set forth in Table A ), both of which are mammalian enzyme(s) (eg, Can be recognized and cleaved by mammalian protease(s) For example, in some cases, the first and second cleavage sequences can be recognized and cleaved by the same enzyme or the same set of enzymes. As such, in some cases, the first and second cleavage sequences may be recognized and cleaved by a different enzyme or set of different enzymes. The first cleavage sequence contains a first cleavable linkage; and to the first cleavage sequence The second cleavage sequence that is C-terminal to contains a second cleavable linkage The first and second cleavable linkages (e.g., indicated by hyphens (-) in Table A ) are exemplary reporter polypeptides An exemplary reporter polypeptide is cleaved with the corresponding enzyme(s) for which both the first and second cleavage sequences are substrates, thereby dividing the N-terminal fragment (N-terminal to the first cleavable linkage), the center Fragments (between the first and second cleavable bonds) and C-terminal fragments (C-terminal to the second cleavable bond) can be obtained N-terminal, central or C-terminal fragments (if present) ) (eg, any set forth in Table A ) or a derivative thereof may serve as a peptide biomarker sequence. The first or second cleavage sequence (eg, any set forth in Table A ) may be used to activate Can be incorporated into the release segment of a possible therapeutic agent (eg, any described herein).
Figure 2 illustrates the nomenclature of a peptide substrate for cleavage and its cleavable linkages. An exemplary peptide substrate comprises eight contiguous amino acid residues, four of which (from N-terminus to C-terminus, with side chain groups in the order R ₄ , R ₃ , R ₂ and R ₁ ) are cleaved It is immediately N-terminal to the bond likely and the four amino acid residues (from N-terminus to C-terminus, with side chain groups in the order R' ₁ , R' ₂ , R' ₃ , and R' ₄ ) are susceptible to cleavage. It is directly C-terminal for easy binding. For example, mammalian proteases can recognize up to four residues on either side of a cleavable bond. Upon cleavage, an exemplary peptide substrate separates into an N-terminal proteolytic fragment and a C-terminal proteolytic fragment. The four amino acid residues immediately N-terminal to the cleavable linkage in the exemplary peptide substrate form the C-terminus of the N-terminal proteolytic fragment; Four amino acid residues immediately C-terminal to the cleavable linkage in the exemplary peptide substrate form the N-terminus of the C-terminal proteolytic fragment.
3 illustrates the structural arrangement of an exemplary activatable antibody (AA) composition comprising an antibody or fragment thereof, a masking moiety (MM) and a releasing segment (RS).
4 is an exemplary activatable antibody complex in which cross-masking occurs such that target binding by both the antibody or fragment thereof is attenuated in the uncleaved state and target binding is increased upon cleavage of the release segment (RS), allowing the complex to be degraded. (AAC) Illustrates the structural arrangement of the composition. In this figure, the two antibodies or fragments thereof are referred to as antibody domain 1 (ABD1) and antibody domain 2 (ABD2), respectively.
5 illustrates the structural arrangement of an exemplary activatable antibody complex (AAC) composition comprising two antibodies or fragments thereof, a masking moiety (MM) and a releasing segment (RS).
6 illustrates the structural arrangement of an exemplary activatable antibody complex (AAC) composition comprising four antibodies or fragments thereof, two masking moieties (MM) and three emissive segments (RS).
7 illustrates the structural arrangement of an exemplary activatable antibody composition (AA) comprising one antibody or antibody fragment (AB), two masking moieties (MM) and two release segments (RS).
8 illustrates the structural arrangement of an XTENylated protease-activated T-cell engager (XPAT). Exemplary XPATs include two binding moieties, each linked to the XTEN via an emissive segment.
9 illustrates the results of mammalian protease cleavage of release segments with sequences similar to those found in collagen I. Cleavage sites are identified with an asterisk (★), with portions of the same sequence as the underlined collagen sites. A sequence engineered not to be recognized or cleaved by a protease that recognizes a collagen-derived cleavage site is presented as 818-NonClv (RSR-3058), and amino acids different from the collagen sequence are shown in black.

In various cancer treatment modalities, agents have been created that can be conditionally activated in the tumor microenvironment. However, there remains a need to develop more accurate and robust methods for predicting whether administration of these therapies will actually result in therapeutic responses and outcomes upon administration of prodrugs or other activatable compositions. It is recognized that there is a series of events that lead to the metastatic growth of cancer cells. A central factor in these events is the interaction between cancer cells and the microenvironment in which tumor cells proliferate, form new blood vessels, leave the primary tumor base and finally enter and persist in secondary sites of metastatic tumor growth. The extracellular matrix (ECM) of the tumor microenvironment is composed of various macromolecules including collagen and glycoproteins. The basement membrane of the ECM is mostly formed by type IV collagen, but type I and III collagen are the most abundant proteins of the basic interstitial matrix. In healthy tissue, the ECM undergoes continuous remodeling, primarily mediated by matrix-metalloproteinases (MMPs), with matrix degradation being balanced by protein formation. This controlled remodeling of the ECM is hampered in cancer development and progression.

During MMP-mediated ECM degradation, small fragments of ECM conversion products are produced and released into the bloodstream. Several studies have shown that serum levels of collagen degradation fragments are elevated in cancer patients compared to healthy controls. Bageret et al. found that levels of MMP-degraded collagen types I, III, and IV (i.e., C1M, C3M, and C4M, respectively; Cancer Biomark. 2015;15:783-788) were 1.5- to 6-fold higher in ovarian and breast cancer patients than in controls. found higher. In the present invention, it has been demonstrated that cleavage of ECM by MMP results in cleavage products that are very similar to the MMP cleavage site of the protease-cleavable linker in XPAT. The data presented herein demonstrates that the protease cleavable linker used in the XPAT of the present invention is cleaved more efficiently by purified MMP than ECM. Thus, it has been shown that the presence of ECM peptides in cancer patients can serve as an indicator that the patient's tumor has a microenvironment with appropriate protease (eg, MMP) activity capable of cleaving protease cleavable linkers in XPAT. . In this way, the presence of ECM peptides in a sample of a cancer patient predicts whether a given patient or tumor can cleave XPAT and thus result in treatment of the tumor. This enables a personalized approach to determining whether XPAT will be cleaved in a given tumor type by determining whether a subject with that tumor type has high plasma levels of a particular cleavage product(s) derived from the extracellular matrix.

Before describing embodiments of the present disclosure, it should be understood that these embodiments are provided by way of example only and that various alternatives to the embodiments of the disclosure described herein may be used in practicing the present invention. Numerous variations, alterations, and substitutions will now occur to those skilled in the art without departing from the invention.

Unless defined otherwise, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention belongs. Although methods and materials similar or equivalent to those described herein may be used in the practice or testing of the present invention, suitable methods and materials are described below. In case of conflict, the patent specification, including definitions, will control. Also, the materials, methods, and examples are illustrative only and are not intended to be limiting. Numerous variations, alterations, and substitutions will now occur to those skilled in the art without departing from the invention.

Justice

In the context of this application, the following terms have the meanings assigned to them unless otherwise specified:

As used throughout the specification and claims, the terms “a,” “an,” and “the” generally refer to “at least one,” “at least a first,” except where an upper limit is specifically recited hereinafter. , "at least one" or "a plurality of" is used to mean the recited component or step. For example, “cleavage sequence” as used herein means “at least a first cleavage sequence” but includes a plurality of cleavage sequences. Operable limits and parameters of combinations, such as amounts of any single agent, will be known to those skilled in the art in light of this disclosure.

The term “activatable,” as used herein with reference to a therapeutic agent, generally means that the activity or bioactivity of the therapeutic agent is enhanced upon activation, for example, through a physical, chemical or physiological process (eg, enzymatic processes and metabolic processes). means it can be

As used herein, the term “activatable therapeutic agent” generally refers to an activity or bioactivity that can be enhanced upon activation, for example, through physical, chemical or physiological processes (eg, enzymatic processes and metabolic processes). refers to the treatment available. For example, the term “activatable therapeutic agent” refers to an inactive (or less active) agent that is configured to be activated (ie in vitro, in vivo or ex vivo) in an active (or more active) state (at least in an inactive embodiment prior to activation). condition (in one aspect at least inactive). As another example, the term “activatable therapeutic agent” may refer to an active therapeutic agent (at least active in one aspect), the activity or bioactivity of which may be further enhanced (i.e., in vitro, in vivo or ex vivo). ). Non-limiting examples of activatable therapeutic agents include prodrugs, probodies and promoieties.

The term "polypeptide". “Peptide” and “protein” are used interchangeably herein to generally refer to polymers of amino acids of any length. Polymers may be linear or branched, may contain modified amino acids, and may be interrupted by non-amino acids. The term also encompasses amino acid polymers modified, for example, by disulfide bond formation, glycosylation, lipidation, acetylation, phosphorylation, or any other manipulation, such as conjugation with a labeling component.

As used herein with reference to the structure of a polypeptide, "N-terminus" (or "amino terminus") and "C-terminus" (or "carboxyl terminus") generally refer to the amino and carboxyl ends, respectively, of a polypeptide. refers to the end

The term "sequence at the N-terminal end" as used herein with reference to a polypeptide or polynucleotide sequence of interest generally refers to the sequence of other amino acids or nucleotides preceding the sequence at the N-terminal end of the polypeptide or polynucleotide sequence of interest, generally at the N-terminal end. This means that there are no residues. The term "sequence at the C-terminal end" as used herein with reference to a polypeptide or polynucleotide sequence of interest generally refers to the sequence of other amino acids or nucleotides following the sequence at the C-terminal end in the polypeptide or polynucleotide sequence at the C-terminal end. means there is no

The terms "non-naturally occurring" and "non-naturally occurring" are used interchangeably herein. The terms “non-naturally occurring” or “non-naturally occurring” as used herein with reference to a therapeutic agent generally means that the agent is not biologically derived from a mammal (including but not limited to humans). The term "non-naturally occurring" or "non-natural" as applied herein and applied to a sequence means a polypeptide that has no counterpart, is not complementary, or does not have a high degree of homology to wild-type or naturally occurring sequences found in mammals. or a polynucleotide sequence. For example, a non-naturally occurring polypeptide or fragment may have no more than 99%, 98%, 95%, 90%, 80%, 70%, 60%, 50% amino acid sequence identity compared to its native sequence when properly aligned. can share

As used herein, the term “antibody” generally refers to an immunoglobulin molecule or any fragment thereof that reacts immunologically with an antigen of interest. For example, an antibody fragment may be of a smaller molecular size and in a single chain format while retaining the ability to bind ligand. The term "antibody" is used herein in the broadest sense and includes monoclonal antibodies, polyclonal antibodies, multispecific antibodies (eg, bispecific antibodies) and antibody fragments so long as they exhibit the desired antigen-binding activity, but hereby A variety of antibody structures are included, but not limited to. Full-length antibodies can be, for example, monoclonal, recombinant, chimeric, deimmunized, humanized and human antibodies.

A "variant" as applied to a biologically active protein is a protein with sequence homology to a natural biologically active protein that retains at least some of the therapeutic and/or biological activity of the biologically active protein. For example, variant proteins share at least 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98% or 99% amino acid sequence identity compared to a reference biologically active protein. can do. As used herein, the term "biologically active protein variant" includes a protein that is intentionally modified and retains activity, for example, through site-directed mutagenesis, synthesis of the coding gene, insertion, or accidental mutation.

The term “sequence variant” refers to a polypeptide that has been altered compared to its natural or original sequence by one or more amino acid insertions, deletions or substitutions. Insertions can be located at one or both ends of the protein and/or within an internal region of the amino acid sequence. A non-limiting example is the substitution of an amino acid in XTEN with a different amino acid. In deletion variants, one or more amino acid residues within a polypeptide as described herein are removed. Deletion variants thus include all fragments of the described polypeptide sequences. In substitutional variants, one or more amino acid residues of a polypeptide are removed and replaced with alternative residues. In one aspect, the substitution is conservative in nature and conservative substitutions of this type are well known in the art. With respect to antibodies or biologically active polypeptides, sequence variants will each retain at least some of the binding affinity or biological activity of the unmodified polypeptide.

The term "moiety" refers to a component of a larger component or intended to be included in a larger component, eg, a proteinaceous portion joined as a contiguous or non-contiguous sequence to a larger polypeptide. Larger constituent moieties can impart desired functionality. For example, an antibody fragment may be of a smaller molecular size and in a single chain format while retaining the ability to bind ligand. A masking moiety (including but not limited to extended recombinant polypeptide (XTEN)) may impart the function of increasing the molecular weight and/or half-life of the resulting larger construct to which the masking moiety is associated.

The terms "binding domain" and "binding moiety" are used interchangeably herein and each refer to a specific binding affinity for an antigen (eg, an effector cell antigen, or a tumor specific marker or antigen of a target cell). refers to a moiety having

As used herein, “releasing segment” or “RS” generally refers to a peptide having one or more cleavage sites in sequence that can be recognized and cleaved by one or more mammalian enzymes (eg, one or more proteases).

As used herein, a "peptide substrate" is generally recognized by an enzyme (e.g., a mammalian protease) to induce cleavage at a peptide bond (or corresponding peptide bonds) within the peptide substrate, prior to cleavage of the peptide bond ( or a scissile bond) that causes two consecutive amino acid residues linked by a bond to separate upon cleavage. As used herein, “cleavable linkage” refers to a peptide bond that links consecutive amino acids through an amide linkage that can be (or is cleaved) generally cleaved by an enzyme (eg, a mammalian protease). For example, in the context of a peptide substrate, the cleavable bond splits the peptide substrate into a C-terminal proteolytic fragment (or C-terminal fragment) and an N-terminal proteolytic fragment (or N-terminal fragment), wherein The C-terminal proteolytic fragment (or C-terminal fragment) is N-terminal to the cleavable bond in the peptide substrate and the N-terminal proteolytic fragment (or N-terminal fragment) is N-terminal to the cleavable bond in the peptide substrate. It is C-terminus. For example, the (presumptive) cleavable linkage of each cleavage sequence listed in Table A is indicated by a hyphen (-).

As used herein, the term “fragile bond” generally refers to a peptide bond between two amino acids that can be cleaved by one or more proteases.

As used herein, the term "mammalian protease" is normally present in bodily fluids, cells, and tissues and will be found at higher levels in certain target tissues or cells of mammals, such as diseased tissues (eg, tumors). proteases that can

The term “within” when referring to linking of a first polypeptide to a second polypeptide refers to an additional component linking the N-terminus of the first or second polypeptide to the C-terminus of the second or first polypeptide, respectively. Linkage or fusion and insertion of a first polypeptide into the sequence of a second polypeptide. For example, when an RS component is linked “within” a recombinant polypeptide, the RS can be linked to the N-terminus, C-terminus, or inserted between any two amino acids of the XTEN polypeptide.

The term “directly linked” as used herein with reference to a therapeutic agent generally refers to a structure in which a moiety is linked or attached to another moiety without an intervening tether. The term “indirectly linked” as used herein with reference to a therapeutic agent generally refers to a structure in which a moiety of a therapeutic agent is connected or attached to another moiety of a therapeutic agent through an intervening tether. The terms "linkage," "linked," and "linking," as used herein with reference to therapeutic agents, generally include both covalent and non-covalent attachment of one moiety of a therapeutic agent to another moiety of a therapeutic agent.

"Activity" (e.g., "bioactivity") as applied to the form(s) of a composition provided herein generally refers to receptor binding, antagonist activity, agonist activity, as measured by in vitro, ex vivo or in vivo assays. , a cell or physiological response, cell lysis, cell death, or an effect generally known in the art for an effector component of a composition, or an action or effect, including but not limited to, a clinical effect.

As used herein, “effector cell” includes any eukaryotic cell capable of conferring an effect on a target cell. For example, an effector cell can induce loss of membrane integrity, nuclear condensation, nuclear collapse, apoptosis, lysis, and/or death of a target cell. In another example, an effector cell is capable of inducing division, growth, differentiation or otherwise altering signal transduction of a target cell.

"Effector cell antigen" means a molecule expressed by an effector cell including without limitation cell surface molecules such as proteins, glycoproteins or lipoproteins. An effector cell antigen can serve as the binding counterpart of a binding moiety of a recombinant polypeptide of interest.

As used herein, the term “ELISA” refers to an enzyme-linked immunosorbent assay as described herein or otherwise known in the art.

A “host cell” generally includes an individual cell or cell culture that can be or is a recipient for a vector of interest into which an exogenous nucleic acid as described herein has been introduced. A host cell includes the progeny of a single host cell. Progeny may not necessarily be completely identical (in morphology or genome in total DNA complement) to the original parent cell due to natural, accidental or deliberate mutation. Host cells include cells transfected in vivo with a vector of the present disclosure.

The term "isolated" when used to describe the various polypeptides disclosed herein generally refers to a polypeptide that has been identified and separated and/or recovered from a component of its natural environment or from a more complex mixture (eg, during protein purification). . Contaminant components of its natural environment are materials that would typically interfere with diagnostic or therapeutic uses for the polypeptide, and may include enzymes, hormones, and other proteinaceous or nonproteinaceous solutes. As will be apparent to those skilled in the art, non-naturally occurring polynucleotides, peptides, polypeptides, proteins, antibodies or fragments thereof do not require "isolation" to distinguish them from their naturally occurring counterparts. Also, "enriched", "isolated" or "diluted" polynucleotides, peptides, polypeptides, proteins, antibodies or fragments thereof are naturally occurring in that the concentration or number of molecules per volume is generally greater than that of their naturally occurring counterparts. Indistinguishable from its occurrence counterpart. Generally, a polypeptide produced by recombinant means and expressed in a host cell is considered "isolated".

An "isolated nucleic acid" is a nucleic acid molecule that has been identified and separated from at least one contaminating nucleic acid molecule that is normally associated in a natural source of a polypeptide-encoding nucleic acid. For example, an isolated polypeptide-encoding nucleic acid molecule is different from the form or environment found in nature. Thus, an isolated polypeptide-encoding nucleic acid molecule is distinguished from a particular polypeptide-encoding nucleic acid molecule present in natural cells. However, an isolated nucleic acid molecule encoding a polypeptide includes a nucleic acid molecule encoding a polypeptide contained in cells that normally express the polypeptide, for example when the nucleic acid molecule is in a chromosomal or extrachromosomal location different from that of natural cells.

A "chimeric" protein or polypeptide contains at least one fusion polypeptide comprising at least one region at a different location in sequence than it occurs in nature. The regions may normally exist in separate proteins and be joined into a fusion polypeptide, or they may normally exist in the same protein but are placed in a new arrangement in a fusion polypeptide. Chimeric proteins can be produced, for example, by chemical synthesis or by recombinantly creating and translating a polynucleotide in which the peptide regions are encoded in a desired relationship.

The terms “fused” and “fusion” are used interchangeably herein and refer to the linking of two or more peptide or polypeptide sequences together by recombinant means. A "fusion protein" or "chimeric protein" comprises a first amino acid sequence linked by nature to a second amino acid sequence that is not linked in nature.

“Uncut” and “uncut” are used interchangeably herein and refer to a polypeptide that has not been digested or cleaved by a protease such that the polypeptide remains intact.

“XTENized” is used to refer to a peptide or polypeptide that has been modified by linking or fusing one or more XTEN polypeptides (described below) to the peptide or polypeptide by recombinant or chemical cross-linking means.

"Crosslinking" and "conjugation" are used interchangeably herein and refer to the covalent bonding of two different molecules by a chemical reaction. Crosslinking can occur in one or more chemical reactions as is known in the art.

In the context of a polypeptide, a "linear sequence" or "sequence" is a sequence of amino acids in a polypeptide in the amino to carboxyl terminal (N-terminus to C-terminus) direction, wherein the residues adjacent to each other in the sequence are contiguous in the primary structure of the polypeptide. is the order of A “partial sequence” is a linear sequence of a portion of a polypeptide known to contain additional residues in one or both directions.

"Heterologous" means derived from an individual that is genotyped distinct from the rest of the individuals being compared. For example, a glycine-rich sequence removed from the native coding sequence and operably linked to a coding sequence other than the native sequence is a heterologous glycine-rich sequence. The term "heterologous" as applied to a polynucleotide or polypeptide means that the polynucleotide or polypeptide is derived from an individual whose genotype is distinct from the rest of the individuals to which it is being compared.

The terms "polynucleotide", "nucleic acid", "nucleotide" and "oligonucleotide" are used interchangeably. They refer to nucleotides of any length and include single nucleic acids and multiple nucleic acids, either deoxyribonucleotides or ribonucleotides, or their analogues. Polynucleotides can have any three-dimensional structure and can perform any function, known or unknown. The following are non-limiting examples of polynucleotides: coding or non-coding regions of genes or gene fragments, loci defined in linkage analysis, exons, introns, messenger RNA (mRNA), transfer RNA, ribosomal RNA, ribozymes, cDNA, Recombinant polynucleotides, branched polynucleotides, plasmids, vectors, isolated DNA of any sequence, isolated RNA of any sequence, nucleic acid probes and primers. A polynucleotide may include modified nucleotides, such as methylated nucleotides and nucleotide analogues. If present, modifications to the nucleotide structure may be provided before or after assembly of the polymer. The sequence of nucleotides may be interrupted by non-nucleotide components. The polynucleotide may be further modified after polymerization, for example by conjugation with a labeling component.

As used herein, the term "reporter polypeptide(s)" refers to a human polypeptide(s) capable of acting in certain circumstances to generate a detectable signal that can be identified and characterized in a cell, organ, tissue or outside the body of a subject. ) or protein(s) (e.g., enzymatically digested to produce detectable peptide sequence(s)). For example, a "reporter polypeptide" can be a human protein that can be cleaved by a protease(s) that can also cleave activatable therapeutic agent(s) (eg, those described below) comprising a peptide substrate. . Non-limiting examples of peptide substrates include those described in the “Release Segment (RS)” section below.

The term “complement of a polynucleotide” refers to a polynucleotide molecule that has a complementary sequence of bases and reverse orientation compared to a reference sequence such that it can hybridize with the reference sequence with full fidelity.

“Recombinant” as applied to a polynucleotide means that the polynucleotide is the product of various combinations of recombination steps, which may include cloning, restriction and/or linking steps, and other procedures that result in expression of a recombinant protein in a host cell.

The terms "gene" and "gene segment" are used interchangeably herein. They represent polynucleotides containing at least one open reading frame capable of encoding a particular protein after being transcribed and translated. A gene or gene fragment may be genomic or cDNA, as long as the polynucleotide contains at least one open reading frame capable of covering the entire coding region or segment thereof. A "fusion gene" is a gene composed of at least two heterologous polynucleotides linked together.

The terms “homology” or “homologous” or “identity” interchangeably refer to sequence similarity between two or more polynucleotide sequences or between two or more polypeptide sequences. When using a program such as BestFit to determine sequence identity, similarity, or homology between two different amino acid sequences, the default settings can be used, or an appropriate scoring matrix such as blossum45 or blossum80 can be selected to determine identity, similarity, or homology. Homology scores can be optimized. Preferably, homologous polynucleotides hybridize under stringent conditions as defined herein and have at least 70%, preferably at least 80%, more preferably at least 90%, even more preferably at least 90%, compared to their sequences when optimally aligned. preferably 95%, more preferably 97%, more preferably 98%, even more preferably 99% sequence identity. Homologous polypeptides have at least 70%, preferably at least 80%, even more preferably at least 90%, even more preferably at least 95-99% identical sequence identity to sequences of similar length when optimally aligned. .

The terms "percent identity", percent sequence identity, and "% identity" as applied to polynucleotide sequences refer to the percentage of residue identity between at least two polynucleotide sequences aligned using a standardized algorithm. These algorithms can insert gaps into the sequences being compared to optimize the alignment between the two sequences in a standardized and reproducible manner, thus achieving a more meaningful comparison of the two sequences. Percent identity is measured over the length of the entire defined polynucleotide sequence, or over a short length, e.g., over the length of a fragment taken from a defined larger polynucleotide sequence, e.g., at least 45, at least 60 , at least 90, at least 120, at least 150, at least 210, or at least 450 contiguous residue fragments. It should be understood that these lengths are exemplary only, and that any fragment length supported by a sequence set forth herein in a table, figure or sequence listing may be used to describe a length at which percent identity can be determined. The percentage of sequence identity is determined by comparing two optimally aligned sequences over a comparison window, determining the number of matching positions (where identical residues occur in both polypeptide sequences), and determining the number of matching positions within the comparison window. It is calculated by dividing by the total number of positions (i.e. window size) and multiplying the result by 100 to yield the percentage of sequence identity. When comparing sequences of different lengths, the shortest sequence defines the length of the comparison window. Conservative substitutions are not considered when calculating sequence identity.

With respect to the polypeptide sequences identified herein, "percent (%) sequence identity" and "percent (%) identity" refer to aligning the sequences and introducing gaps as necessary to achieve the maximum percentage of sequence identity, and any conservation It is defined as the percentage of amino acid residues in the query sequence that are identical to the amino acid residues of a second reference polypeptide sequence or portion thereof of similar length, after generating the optimal alignment by not considering the redundant substitution as part of the sequence identity. Alignment for the purpose of determining percent amino acid sequence identity can be accomplished in a variety of ways that are within the skill of the art, for example using publicly available computer software such as BLAST, BLAST-2, ALIGN or Megalign (DNASTAR) software. can One skilled in the art can determine appropriate parameters for measuring alignment, including any algorithms needed to achieve optimal alignment over the entire length of the sequences being compared. Percent identity is measured over the length of the entire defined polypeptide sequence, or over a short length, e.g., over the length of a fragment taken from a larger defined polypeptide sequence, e.g., at least 15, at least 20, It can measure over a fragment of at least 30, at least 40, at least 50, at least 70, or at least 150 contiguous residues. It should be understood that these lengths are exemplary only, and that any fragment length supported by a sequence set forth herein in a table, figure or sequence listing may be used to describe a length at which percent identity can be determined.

As used herein, the term "expression" refers to the process by which a polynucleotide produces a gene product, such as RNA or polypeptide. This includes, without limitation, transcription of a polynucleotide into messenger RNA (mRNA), transfer RNA (tRNA), small hairpin RNA (shRNA), small interfering RNA (siRNA) or any other RNA product and translation of mRNA into a polypeptide. . Expression produces a "gene product". As used herein, a gene product can be a nucleic acid, eg, a messenger RNA produced by transcription of a gene or a polypeptide translated from a transcript. Gene products described herein are nucleic acids with post-transcriptional modifications, such as polyadenylation or splicing, or post-translational modifications, such as methylation, glycosylation, addition of lipids, association with other protein subunits, or proteolysis. Further included are polypeptides with cleavages.

“Vector” or “expression vector” are used interchangeably and refer to a nucleic acid molecule that transfers an inserted nucleic acid molecule into and/or between host cells, preferably autonomously replicating in a suitable host. The term includes vectors that function primarily to insert DNA or RNA into cells, clones of vectors that function primarily for the replication of DNA or RNA, and expression vectors that function primarily for the transcription and/or translation of DNA or RNA. do. Vectors that provide one or more of the above functions are also included. An “expression vector” is a polynucleotide that can be transcribed and translated into polypeptide(s) when introduced into an appropriate host cell. "Expression system" generally means a suitable host cell composed of an expression vector capable of functioning to produce a desired expression product.

The terms “ _t½ ”, “half-life”, “elimination half-life”, “elimination half-life”, and “circulation half-life” are used interchangeably herein and, as used herein, are generally ln(2) /K _el refers to the calculated elimination half-life. K _el is the terminal elimination rate constant calculated by linear regression of the terminal linear portion of the log concentration versus time curve. Half-life generally refers to the time required for half of the amount of a substance deposited upon administration to a living organism to be metabolized or eliminated by normal biological processes. When a clearance curve for a given polypeptide is constructed as a function of time, the curve is generally biphasic with a rapid α-phase and a longer β-phase. The typical β-phase half-life of human antibodies in humans is 21 days. Half-life can be measured using time-stamped samples derived from any bodily fluid, but is most commonly measured in serum or plasma samples.

The term “molecular weight” generally refers to the sum of the atomic weights of the constituent atoms of a molecule. Molecular weight can be determined theoretically by summing the atomic masses of the constituent atoms of the molecule. When applied in the context of a polypeptide, molecular weight is calculated by adding the molecular weight of each type of amino acid in the composition, based on the amino acid composition, or by extrapolation from comparison to molecular weight standards in SDS electrophoretic gels. The calculated molecular weight of a molecule may differ from the "apparent molecular weight" of a molecule, which generally refers to the molecular weight of a molecule as determined by one or more analytical techniques. “Apparent molecular weight factor” and “apparent molecular weight” are related terms, and when used in the context of a polypeptide, these terms refer to a measure of the relative increase or decrease in apparent molecular weight exhibited by a particular amino acid or polypeptide sequence. Apparent molecular weight may be determined using size exclusion chromatography (SEC) or similar methods, for example by comparison to globular protein standards as measured in "apparent kD" units. The apparent molecular weight factor is the ratio between apparent molecular weight and “molecular weight”; The latter is calculated by addition based on amino acid composition as described above, or extrapolated from comparison to molecular weight standards in SDS electrophoretic gels. Determination of the apparent molecular weight and apparent molecular weight factor is described, inter alia, in US Pat. No. 8,673,860.

The term “hydrodynamic radius” or “Stokes radius” is the effective radius (R _h in nm) of a molecule in a solution measured assuming that the molecule is a body that moves through the solution and resists the viscosity of the solution. In embodiments of the present disclosure, a measure of the hydrodynamic radius of an XTEN polypeptide is correlated with a more intuitive measure, the "apparent molecular weight factor". A protein's "hydrodynamic radius" affects its rate of diffusion in aqueous solution and its ability to migrate in a gel of macromolecules. The hydrodynamic radius of a protein is determined not only by its molecular weight, but also by its structure, including shape and compactness. Methods for determining the hydrodynamic radius are well known in the art, particularly by use of size exclusion chromatography (SEC) as described in U.S. Pat. Nos. 6,406,632 and 7,294,513. Most proteins have a spherical structure, which is the most compact three-dimensional structure a protein can have with the smallest hydrodynamic radius. Some proteins adopt a random and open, unstructured or 'linear' conformation, resulting in much larger hydrodynamic radii compared to typical globular proteins of similar molecular weight.

"Physiological conditions" means a set of conditions in a living host, including temperature, salt concentration, pH, and in vitro conditions that mimic those of a living subject. A host of physiologically relevant conditions for use in in vitro assays have been established. Generally, physiological buffers contain physiological concentrations of salt and are adjusted to a neutral pH ranging from about 6.5 to about 7.8, preferably from about 7.0 to about 7.5. A variety of physiological buffers are described in Sambrook et al. (2001)]. Physiologically relevant temperatures range from about 25°C to about 38°C, preferably from about 35°C to about 37°C.

The term "binding moiety" is used herein in its broadest sense and specifically refers to an antigen or ligand, such as a cell surface receptor, target cell marker, or antigen or glycoprotein, oligonucleotide, enzyme substrate, antigenic determinant, or tissue or It is intended to include categories of cytokines, cellular receptors, antibodies or antibody fragments that have a specific affinity for a binding site that may be present on or on the surface of a cell.

As used herein, the term "monoclonal antibody" refers to an antibody obtained from a population of substantially homogeneous antibodies, i.e., an individual antibody comprising a population may contain variant antibodies, e.g., naturally occurring mutations, or may be derived from a preparation of a monoclonal antibody. Except for variant antibodies that arise during production that are identical and/or bind to the same epitope, such variants are generally present in minor amounts. In contrast to polyclonal antibody preparations, which typically contain different antibodies directed against different determinants (epitopes), each monoclonal antibody in a monoclonal antibody preparation is directed against a single determinant of the antigen. Thus, the modifier "monoclonal" indicates the character of the antibody as being obtained from a substantially homogeneous population of antibodies, and is not to be construed as requiring production of the antibody by any particular method. For example, monoclonal antibodies used in accordance with the present invention include, but are not limited to, hybridoma methods, recombinant DNA methods, phage-display methods, and methods using transgenic animals comprising any human immunoglobulin locus or part thereof. It can be made by a variety of non-limiting techniques, and such methods and other exemplary methods for making monoclonal antibodies are known in the art or described herein.

As used herein, “antibody fragment” generally refers to a molecule other than an intact antibody that comprises a portion of an intact antibody and binds an antigen to which the intact antibody binds. Examples of antibody fragments include Fv, Fab, Fab', Fab'-SH, F(ab')2, diabodies, single chain diabodies, linear antibodies, nanobodies (including single chain camelid antibodies), single domain antibodies or Also known as V _HH ) single chain variable fragment (scFv) antibody molecules and multispecific antibodies formed from antibody fragments.

"scFv" or "single chain fragment variable region", as used interchangeably herein, is a region of a variable heavy chain ("VH") and variable light chain ("VL"), or VH or VL, linked together by a short flexible peptide linker. Refers to a form of antibody fragment comprising two copies of a chain. An scFv is not actually a fragment of an antibody, but is a fusion protein of the variable regions of the heavy (VH) and light (VL) chains of an immunoglobulin, and in an N-terminal to C-terminal direction in E. coli or mammalian cell(s), the VL Can be readily expressed in functional forms of -VH or VH-VL.

The terms “antigen,” “target cell marker” and “ligand” are used interchangeably herein to refer to a binding moiety, structure or binding to which an antibody, antibody fragment or molecule based on an antibody fragment binds or has binding specificity thereto. refers to the determinant.

The term “epitope” refers to a specific site on an antigenic molecule to which an antibody, antibody fragment or binding moiety binds. An epitope is the ligand of an antibody, antibody fragment or binding moiety.

The term “diagnostic reagent” is used herein to refer to any reagent used in vivo or in vitro for the detection or screening of a particular disease. This includes, but is not limited to, assays, antibodies, tests, nucleic acid-based tests including RT-PCR, and laboratory tests.

As used herein, "CD3" or "cluster of differentiation 3" refers to all known CD3 subunits, e.g., CD3 epsilon, CD3 delta, CD3 gamma, CD3 zeta, CD3 alpha and CD3 beta, either individually or in combination. T cell surface antigen CD3 complex, including the form. The extracellular domains of CD3 epsilon, gamma and delta contain immunoglobulin-like domains and are therefore considered part of the immunoglobulin superfamily.

The terms "specific binding" or "specifically binds" or "binding specificity" are used interchangeably herein to refer to a high degree of binding affinity of a binding moiety for its corresponding target. Typically, specific binding measured by one or more assays disclosed herein will have a dissociation constant or K _d of less than about 10 ⁻⁶ M (eg, 10 ⁻⁷ M to 10 ⁻¹² M).

As used herein, the term “affinity” generally refers to the strength of the sum of non-covalent interactions between a single binding site of a molecule (eg an antibody) and its binding partner (eg an antigen). Unless otherwise indicated, “binding affinity” as used herein refers to intrinsic binding affinity that reflects a 1:1 interaction between members of a binding pair (eg, antibody and antigen). The affinity of a molecule X for its partner Y can generally be represented by the dissociation constant (K _d ). “Higher binding affinity” or “increased binding affinity” as used herein means a lower K _d value; For example, 1 x 10 ^-9 M is a greater binding affinity than 1 x 10 ^-8 M, whereas "lower binding affinity" means a greater K _d value; For example, 1 x 10 ^-7 M is a lower binding affinity than 1 x 10 ^-8 M.

“Inhibition constant” or “K _i ” are used interchangeably and refer to the dissociation constant of an enzyme-inhibitor complex or the reciprocal of the binding affinity of an inhibitor to an enzyme.

"Dissociation constant" or "K _d " is used interchangeably and refers to the affinity between a ligand "L" and a protein "P", eg, how tightly the ligand binds to a particular protein. This can be calculated using the formula K _d = [L][P]/[LP], where [P], [L], and [LP] represent the molar concentrations of protein, ligand and complex, respectively. As used herein, the term "k _on " is intended to refer to the on rate constant for the association of an antibody to an antigen to form an antibody/antigen complex, as is known in the art. As used herein, the term "k _off " is intended to refer to the off rate constant for the dissociation of an antibody from an antibody/antigen complex as is known in the art. Binding events can be detected using techniques such as flow cytometry or surface plasmon resonance. The assay may include soluble antigen or receptor molecules or may determine binding to cell expressed receptors. Such assays may include cell-based assays, including assays for proliferation, apoptosis, apoptosis, and cell migration. The binding affinity of a subject composition to a target ligand can be measured in a binding assay or a competitive binding assay, such as a Biacore assay using a chip bound receptor or binding protein or an ELISA assay, as described in U.S. Patent No. 5,534,617, or an assay described in the Examples herein. , radioreceptor assays, reporter gene activity assays, or other assays known in the art. For example, an exemplary reporter gene activity assay can be based on genetically engineered cell(s) generated by stably introducing the relevant gene(s) for the receptor(s) and signaling pathway(s) of interest; As a result, binding to the engineered receptor triggers a signaling cascade leading to activation of the engineered genetic pathway with subsequent production of the signature polypeptide(s) (eg, enzyme). Binding affinity constants are then determined using standard methods, such as Scatchard analysis as described by van Zoelen, et al., Trends Pharmacol Sciences (1998) 19)12):487, or other methods known in the art. can decide

A “target cell marker” is a cell surface receptor, cytokine receptor, antigen, tumor-associated antigen, glycoprotein, oligonucleotide, enzyme substrate, antigenic determinant or binding moiety that can act as a ligand for a target tissue or cell present on the surface of the cell. A molecule expressed by a target cell, including, but not limited to, a binding site capable of binding. Non-limiting examples of target cell markers include the target markers in Table 6 .

The term "target tissue" generally refers to a tissue that is a cause of or is part of a disease condition, such as, but not limited to, cancer or an inflammatory condition. The source of a diseased target tissue is a body organ, tumor, cancer cell or cell that forms a cancer cell population or matrix or is found in association with a cancer cell population, bone, skin, cells that produce cytokines or factors that contribute to the disease state. include

The term “target cell” generally refers to a cell that has a ligand of a binding moiety, an antibody or antibody fragment of a subject composition, and is associated with or causes a disease or pathological condition, including cancer cells, tumor cells and inflammatory cells. . Ligands of target cells are referred to herein as "target cell markers" or "target cell antigens" and include cell surface receptors or antigens, cytokines, cytokine receptors, MHC proteins and cytosolic proteins or exogenously presented peptides; , but not limited thereto. As used herein, “target cells” will not include effector cells.

As used herein, an “immunoassay” generally refers to the reaction of an antibody (or fragment thereof) with its cognate antigen, e.g., the specific binding of an antibody to a protein to determine the presence of a substance in a sample, such as a biological sample. or a biochemical test that measures concentration. Both the presence of antigen or the amount of antigen present can be measured.

As used herein, “mass spectrometer (MS)” generally refers to a device that includes means for ionizing molecules and detecting charged molecules. A mass spectrum generated by a mass spectrometer can be used to identify the molecule(s) of interest based on molar mass. Non-limiting examples of “mass spectrometry (MS)” include any combination with liquid chromatography (LC), such as liquid chromatography with mass spectrometry (LC-MS), liquid chromatography with tandem mass spectrometry (LC-MS). /MS), etc.

As used herein, the terms “treatment” or “treating” or “mitigating” or “improving” are used interchangeably herein. These terms generally refer to an approach for obtaining beneficial or desired results, including but not limited to therapeutic benefit and/or prophylactic benefit. By therapeutic benefit is meant eradication or amelioration of the underlying disorder being treated. In addition, therapeutic benefit is achieved by eradication or amelioration of one or more physiological symptoms or improvement of one or more clinical parameters associated with the underlying disorder, such that improvement is observed in the subject even though the subject may still suffer from the underlying disorder. For prophylactic benefit, the composition can be administered to a subject at risk of developing a particular disease, or to a subject reporting one or more physiological symptoms of a disease, even though a diagnosis of the disease may not have been made.

As used herein, "therapeutic effect" or "therapeutic benefit" generally refers to a disease in a human or other animal resulting from administration of a polypeptide of the present disclosure other than the ability to induce production of antibodies against antigenic epitopes possessed by biologically active proteins. physiological effect, including but not limited to, the alleviation, amelioration or prevention of, or improvement of one or more clinical parameters associated with an underlying disorder, or otherwise enhancing the physical or mental well-being of a human or other animal. For prophylactic benefit, a composition may be provided to a subject at risk of developing a particular disease, a recurrence of a previous disease, a condition or symptom of a disease, or reporting one or more physiological symptoms of a disease, even if a diagnosis of the disease may not have been made. can be administered to a subject.

As used herein, the terms "therapeutically effective amount" and "therapeutically effective dose" generally refer to any symptom, aspect, measured parameter or characteristic of a disease state or condition when administered to a subject in single or repeated doses. Refers to the amount of a drug or biologically active protein, alone or as part of a polypeptide composition, that can have a detectable beneficial effect. These effects need not be absolute to be beneficial. Determination of a therapeutically effective amount is well within the ability of those skilled in the art, especially in light of the detailed disclosure provided herein.

The term “equimolar dose” generally means that the amount of a substance administered to a subject has an equivalent molar amount based on the molecular weight of the substance used in the dose.

As used herein, the term "therapeutically effective and non-toxic dose" is defined herein generally high enough to cause depletion of a tumor or cancer cells, elimination of a tumor, shrinkage of a tumor, or stabilization of a disease with no or essentially no significant toxic effect in a subject. Refers to an acceptable dose of the composition as described. Such therapeutically effective and non-toxic doses can be determined by dose escalation studies described in the art and should be below doses that cause serious side effects.

The terms “cancer” and “cancerous” refer to or describe the physiological condition of a mammal that is typically characterized by unregulated cell growth/proliferation.

composition

remedy

In some embodiments, a release segment (RS) (e.g., described in the Biologically Active Moiety section below or elsewhere herein) directly or indirectly linked to a biologically active moiety (BM). Provided herein are therapeutic agents (or activatable therapeutic agents, or non-natural activatable therapeutic agents) including, for example, those described in the release segments section below or elsewhere herein). A biologically active moiety (BM) can be a biologically active peptide (BP) (eg, described in the Biologically Active Moieties section below or elsewhere herein). The release segment (RS) is a peptide substrate (e.g., in the release segment section below) that is susceptible to cleavage by a mammalian protease (e.g., described below or elsewhere herein) at its cleavable linkage. described or described elsewhere herein). The therapeutic agent may further comprise a masking moiety (MM) (e.g., described in the Masking Moiety section below or elsewhere herein) linked directly or indirectly to the emitting segment (RS). . The bioactivity of a therapeutic agent can be enhanced upon cleavage of the peptide substrate by a mammalian protease (thereby releasing the masking moiety). The therapeutic agent in an uncut state may have a structural arrangement from the N-terminus to the C-terminus of BM-RS-MM or MM-RS-BM. Upon cleavage of the releasing segment (RS), the masking moiety (MM) can be released from the therapeutic agent. The masking moiety (MM) may include an extended recombinant polypeptide (XTEN). The therapeutic agent in an uncut state may have a structural arrangement from the N-terminus to the C-terminus of BM-RS-XTEN or XTEN-RS-BM.

In some embodiments of the therapeutic agent (or activatable therapeutic agent, or non-natural activatable therapeutic agent), where the releasing segment (RS) may be the first releasing segment (RS1), the peptide substrate (of RS1) is the first peptide substrate. and if the cleavable linkage (of RS1) can be the first cleavable linkage, then the therapeutic agent is a second emitting segment (RS2) linked directly or indirectly to the biologically active moiety (BM) (e.g. eg, as described in the Release Segments section below or elsewhere herein). The second emissive segment (RS2) is a second peptide substrate (e.g., hereinafter) for cleavage by a mammalian protease (e.g., described below or elsewhere herein) at a second cleavable linkage. as described in the Release Segment section of or elsewhere herein). The bioactivity of the therapeutic may be enhanced upon cleavage of one or both of the first and second peptide substrates by a mammalian protease (thereby releasing one or both of the first and second masking moieties). The mammalian protease for cleavage of the second release segment (RS2) may be the same as the mammalian protease for cleavage of the first release segment (RS1). The mammalian protease for cleavage of the second release segment (RS2) may be different from the mammalian protease for cleavage of the first release segment (RS1). The second emitting segment RS2 may have the same amino acid sequence as the first emitting segment RS1. The second emitting segment RS2 may have a different amino acid sequence than the first emitting segment RS1. In some embodiments, the cleavable linkage (or the first cleavable linkage, or the second cleavable linkage) is not immediately C-terminal to the methionine residue. In some embodiments, the first cleavable linkage is not immediately C-terminal to the methionine residue. In some embodiments, the second cleavable linkage is not immediately C-terminal to the methionine residue.

In some embodiments of the therapeutic agent (or activatable therapeutic agent, or non-natural activatable therapeutic agent), where the masking moiety (MM) can be the first masking moiety (MM1), the therapeutic agent comprises a second releasing segment (RS2) may further include a second masking moiety (MM2) linked directly or indirectly to (eg, as described in the Masking Moieties section below or elsewhere herein). The therapeutic agent in the uncut state is N-terminus of MM1-RS1-BM-RS2-MM2, MM1-RS2-BM-RS1-MM2, MM2-RS1-BM-RS2-MM1, or MM2-RS2-BM-RS1-MM1 to the C-terminus. Upon cleavage of the second release segment (RS2), the second masking moiety (MM2) can be released from the therapeutic agent. The first masking moiety (MM1) may comprise a first extended recombinant polypeptide (XTEN1). The second masking moiety (MM2) may comprise a second extended recombinant polypeptide (XTEN2). The therapeutic agent in the uncut state is XTEN1-RS1-BP-RS2-XTEN2, XTEN1-RS2-BP-RS1-XTEN2, XTEN2-RS1-BP-RS2-XTEN1, or the N-terminus of XTEN2-RS2-BP-RS1-XTEN1. to the C-terminus.

In some embodiments of the therapeutic agent (or activatable therapeutic agent, or non-natural activatable therapeutic agent), the therapeutic agent comprises a fusion polypeptide (eg, a recombinant fusion protein) or a conjugate (eg, a conjugate linked by chemical conjugation). can do. In some embodiments, the therapeutic agent may be configured for activation in or near a target tissue or cell (eg, described in the Target Tissue or Cell section below or elsewhere herein) of a subject. The therapeutic agent may be an anti-cancer agent (eg, an activatable anti-cancer agent, or a non-natural activatable anti-cancer agent). A therapeutic agent can be configured for activation by one or more mammalian proteases (eg, one or any combination of those described herein).

In some embodiments of the therapeutic agent (or activatable therapeutic agent, or non-natural activatable therapeutic agent), the therapeutic agent may comprise a recombinant polypeptide. A recombinant polypeptide may include a biologically active peptide (BP) and a release segment (RS). A recombinant polypeptide may include a biologically active peptide (BP), a releasing segment (RS) and a masking moiety (MM). The recombinant polypeptide in an uncut state may have a structural arrangement from the N-terminus to the C-terminus of BP-RS-MM or MM-RS-BP. A recombinant polypeptide may comprise a biologically active peptide (BP), a first emitting segment (RS1) and a second emitting segment (RS2). A recombinant polypeptide may comprise a biologically active peptide (BP), a first emissive segment (RS1), a second emissive segment (RS2), a first masking moiety (MM1) and a second masking moiety (MM2). The recombinant polypeptide in the uncleaved state is N- It may have a structural arrangement from terminal to C-terminus. The recombinant polypeptide may include a biologically active peptide (BP), a first emissive segment (RS1), a second emissive segment (RS2), a first extended recombinant polypeptide (XTEN1) and a second extended recombinant polypeptide (XTEN2). . The recombinant polypeptide in the uncleaved state is XTEN1-RS1-BP-RS2-XTEN2, XTEN1-RS2-BP-RS1-XTEN2, XTEN2-RS1-BP-RS2-XTEN1, or N-XTEN2-RS2-BP-RS1-XTEN1. It may have a structural arrangement from terminal to C-terminus.

Emission Segment (RS)

In some embodiments of the therapeutic agent (or activatable therapeutic agent, or non-natural activatable therapeutic agent), the release segment (RS) (or the first release segment (RS1), or the second release segment (RS2) is (each independently) It may contain a peptide substrate that is susceptible to cleavage by mammalian proteases at its cleavable linkage A target in which the release segment (RS) (or the first release segment (RS1), or the second release segment (RS2)) is a peptide substrate. If the tissue or cell is capable of producing a mammalian protease (e.g., as described in the Target Tissue or Cell section below or elsewhere herein), the release segment (RS) (or the first release segment (RS1); or the second emitting segment (RS2)) may (each independently) be cleaved when in proximity to a target tissue or cell (eg, described in the Target Tissue or Cell section below or elsewhere herein).

In some embodiments of the therapeutic agent (or activatable therapeutic agent, or non-natural activatable therapeutic agent), the peptide substrate (or first peptide substrate, or second peptide substrate) is directed to a reporter polypeptide (eg, to a target tissue or cell section below). up to 4, or up to 3, or up to 2 for a cleavage sequence (e.g., those shown in Tables 1(a)-1(j) or Table A ) of those described or described elsewhere herein; or up to one amino acid substitution(s). The peptide substrate (or the first peptide substrate, or the second peptide substrate) can be up to 4, or up to 3, to the cleavage sequence of the reporter polypeptide (eg, those shown in Tables 1(a)-1(j) or Table A ). , or up to 2, or up to 1 amino acid substitution(s). The peptide substrate (or the first peptide substrate, or the second peptide substrate) may comprise an amino acid sequence identical to the cleavage sequence of the reporter polypeptide (eg, those set forth in Tables 1(a)-1(j) or Table A ). . In some embodiments of the therapeutic agent (or activatable therapeutic agent, or non-natural activatable therapeutic agent), the peptide substrate (or the first peptide substrate, or the second peptide substrate) is listed in column II or column III of Table A (or a subset thereof). ) and/or up to 4, or up to 3, or up to 2, or up to 1 amino acid substitutions for groups shown in Tables 1(a)-1(j) (or any subset thereof) It may include an amino acid sequence having (s). The peptide substrate (or the first peptide substrate, or the second peptide substrate) is a sequence set forth in column II or III of Table A (or a subset thereof) and/or Tables 1(a)-1(j) (or any thereof). Subsets of) can include an amino acid sequence with up to 4, or up to 3, or up to 2, or up to 1 amino acid substitution(s) for a group set forth in. The peptide substrate (or the first peptide substrate, or the second peptide substrate) is a sequence set forth in column II or III of Table A (or a subset thereof) and/or Tables 1(a)-1(j) (or any thereof). A subset of) may include the same amino acid sequence as the group shown in. In some embodiments, the peptide substrate (or first peptide substrate, or second peptide substrate) comprises two or three sequences set forth in column II or III (or a subset thereof) of Table A. In some embodiments, when the peptide substrate (or first peptide substrate, or second peptide substrate) comprises two sequences set forth in column II or column III (or a subset thereof) of Table A , the two sequences are in part overlap each other with In some embodiments, when the peptide substrate (or first peptide substrate, or second peptide substrate) comprises two sequences set forth in column II or column III (or a subset thereof) of Table A , the two sequences are mutually do not overlap In some embodiments, when the peptide substrate (or the first peptide substrate, or the second peptide substrate) comprises the three sequences set forth in column II or column III (or a subset thereof) of Table A , two of the three sequences Dogs or all do not overlap with each other. In some embodiments, when the peptide substrate (or the first peptide substrate, or the second peptide substrate) comprises the three sequences set forth in column II or column III (or a subset thereof) of Table A , one of the three sequences partially overlaps with another sequence or with the sequence of both of the other three sequences. In some embodiments, when the peptide substrate (or the first peptide substrate, or the second peptide substrate) comprises the three sequences set forth in column II or column III (or a subset thereof) of Table A , two of the three sequences Dogs partially overlap each other. In some embodiments, when the peptide substrate (or first peptide substrate, or second peptide substrate) comprises three sequences set forth in column II or column III (or a subset thereof) of Table A , each of the three sequences The two partially overlap each other. In some embodiments, when the peptide substrate (or first peptide substrate, or second peptide substrate) comprises three sequences set forth in column II or III (or a subset thereof) of Table A , all three sequences are partially overlap each other. In some embodiments, none of at most 4, at most 3, at most 2, or at most 1 amino acid substitution(s) is a cleavable bond of a sequence set forth in column II or column III (or a subset thereof) of Table A. is not at a position corresponding to the amino acid residue immediately adjacent to In some embodiments, none of up to 4, up to 3, up to 2, or up to 1 amino acid substitution(s) is from a group set forth in Tables 1(a)-1(i) (or any subset thereof). It is not located at a position corresponding to an amino acid residue immediately adjacent to a scissile bond of the selected corresponding sequence. In some embodiments, none of up to 4, up to 3, up to 2, or up to 1 amino acid substitution(s) in a corresponding sequence selected from the group set forth in Table 1(j) (or any subset thereof). It is not in a position corresponding to an amino acid residue immediately adjacent to a cleavable bond. The peptide substrate (or the first peptide substrate, or the second peptide substrate) is 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, or 25 amino acid residues or ranges of any two of the above values. Peptide substrates may contain 6 to 25 or 6 to 20 amino acid residues. Peptide substrates can contain from 6 to 25 amino acid residues. Peptide substrates may contain 6 to 20 amino acid residues. In some embodiments, the peptide substrate contains 7 to 12 amino acid residues. The peptide substrate may comprise amino acids shown in column II or III of Table A (or a subset thereof) and/or fragments of the groups shown in Tables 1(a)-1(j) (or any subset thereof). there is. Fragments of the peptide substrate may contain at least 4 amino acid residues and corresponding cleavable bonds (eg, as shown in Tables 1(a)-1(j) or Table A ). A fragment of a peptide substrate may contain at least 5, at least 6, at least 7, at least 8, at least 9 or at least 10 amino acid residues. In some cases, the portion of the peptide substrate that is N-terminal of the scissile bond is the C-terminal end containing 4 to 10 amino acid residues of the sequence set forth in column IV or V of Table A (or a subset thereof). may have up to 4, or up to 3, or up to 2, or up to 1 amino acid substitution(s) for the sequence of The portion of the peptide substrate that is N-terminal of the scissile bond comprises a sequence at the C-terminal end containing 4 to 10 amino acid residues of the sequence set forth in column IV or V (or a subset thereof) of Table A. can do. In some cases, the portion of the peptide substrate that is N-terminal of the scissile bond is in a sequence at the C-terminal end containing 4 to 10 amino acid residues of the sequence set forth in column IV of Table A (or a subset thereof). may have up to 4, or up to 3, or up to 2, or up to 1 amino acid substitution(s) for The portion of the peptide substrate that is N-terminal of the scissile bond may include a sequence at the C-terminal end containing 4 to 10 amino acid residues of the sequence set forth in column IV of Table A (or a subset thereof). . In some cases, the portion of the peptide substrate that is N-terminal of the scissile bond is in a sequence at the C-terminal end containing 4 to 10 amino acid residues of the sequence set forth in column V of Table A (or a subset thereof). may have up to 4, or up to 3, or up to 2, or up to 1 amino acid substitution(s) for The portion of the peptide substrate that is N-terminal of the scissile bond may include a sequence at the C-terminal end containing 4 to 10 amino acid residues of the sequence set forth in column V of Table A (or a subset thereof). . In some cases, the portion of the peptide substrate that is the C-terminus of the scissile bond is an N-terminal end containing 4 to 10 amino acid residues of a sequence set forth in column V or column VI (or a subset thereof) of Table A. may have up to 4, or up to 3, or up to 2, or up to 1 amino acid substitution(s) for the sequence of The portion of the peptide substrate that is C-terminal of the scissile bond comprises a sequence at the N-terminal end containing 4 to 10 amino acid residues of the sequence set forth in column V or VI (or a subset thereof) of Table A. can do. In some cases, the portion of the peptide substrate that is the C-terminus of the scissile bond is in a sequence at the N-terminal end containing 4 to 10 amino acid residues of the sequence set forth in column V of Table A (or a subset thereof). may have up to 4, or up to 3, or up to 2, or up to 1 amino acid substitution(s) for The portion of the peptide substrate that is the C-terminus of the scissile bond may include a sequence at the N-terminal end containing 4 to 10 amino acid residues of the sequence set forth in column V of Table A (or a subset thereof). . In some cases, the portion of the peptide substrate that is the C-terminus of the scissile bond is in a sequence at the N-terminal end containing 4 to 10 amino acid residues of the sequence set forth in column VI of Table A (or a subset thereof). may have up to 4, or up to 3, or up to 2, or up to 1 amino acid substitution(s) for The portion of the peptide substrate that is the C-terminus of the scissile bond may include a sequence at the N-terminal end containing 4 to 10 amino acid residues of the sequence set forth in column VI of Table A (or a subset thereof). . In some embodiments, where the peptide substrate includes a cleavable bond (for cleavage by one or more mammalian proteases), the peptide substrate does not include a methionine residue immediately N-terminal to the cleavable bond. . In some embodiments, where the peptide substrate includes a plurality of cleavable bonds, the peptide substrate does not include a methionine residue immediately N-terminal to at least one cleavable bond of the plurality of cleavable bonds. . In some embodiments, where the peptide substrate includes a plurality of cleavable bonds, the peptide substrate does not include a methionine residue immediately N-terminal to each cleavable bond of the plurality of cleavable bonds. In some embodiments , the peptide substrate is #279, #280, #282, #283, #298, #299, #302, #303, #305, #307, #308, #349, Does not contain an amino acid sequence selected from the group consisting of #396, #397, #416, #417, #418, #458, #459, #460, #466, #481 and #482 (or any combination thereof) .

(1) a first release segment (RS1) comprising a first peptide substrate and (2) a second release segment (RS2) comprising a second peptide substrate (or activatable therapeutic agent, or non-natural activation In some embodiments, the second peptide substrate is 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, or 25 amino acid residues or ranges of any two of the above values. The second peptide substrate may contain 6 to 25 or 6 to 20 amino acid residues. The second peptide substrate may contain 6 to 25 amino acid residues. The second peptide substrate may contain 6 to 20 amino acid residues. The second peptide substrate may contain 7 to 12 amino acid residues. The second peptide substrate may contain up to 4 peptides for a sequence set forth in column II or III of Table A (or a subset thereof) and/or a group set forth in Tables 1(a)-1(j) (or any subset thereof). or up to 3, or up to 2, or up to 1 amino acid substitution(s). The second peptide substrate may contain up to 4 peptides for a sequence set forth in column II or III of Table A (or a subset thereof) and/or a group set forth in Tables 1(a)-1(j) (or any subset thereof). or up to 3, or up to 2, or up to 1 amino acid substitution(s). The second peptide substrate comprises a sequence set forth in column II or column III of Table A (or a subset thereof) and/or an amino acid sequence identical to a group set forth in Tables 1(a)-1(j) (or any subset thereof). can include In some embodiments, the second peptide substrate comprises two or three sequences set forth in column II or column III of Table A (or a subset thereof). In some embodiments, when the second peptide substrate comprises two sequences set forth in column II or III (or a subset thereof) of Table A , the two sequences (of the second peptide substrate) partially overlap each other. . In some embodiments, when the second peptide substrate comprises two sequences set forth in column II or III (or a subset thereof) of Table A , the two sequences (of the second peptide substrate) do not overlap with each other. In some embodiments, where the second peptide substrate comprises three sequences set forth in column II or III (or a subset thereof) of Table A , two or all of the three sequences (of the second peptide substrate) do not overlap each other In some embodiments, where the second peptide substrate comprises three sequences set forth in column II or III (or a subset thereof) of Table A , one of the three sequences (of the second peptide substrate) is another sequence. or partially overlapping sequences of both of the other three sequences (of the second peptide substrate). In some embodiments, where the second peptide substrate comprises three sequences set forth in column II or III (or a subset thereof) of Table A , two of the three sequences (of the second peptide substrate) are partial to each other. overlapped with In some embodiments, where the second peptide substrate comprises three sequences set forth in column II or III (or a subset thereof) of Table A , then two of each of the three sequences (of the second peptide substrate) are mutually exclusive. partially overlapping. In some embodiments, when the second peptide substrate comprises three sequences set forth in column II or III (or a subset thereof) of Table A , all three sequences (of the second peptide substrate) partially overlap each other. do. In some embodiments, where the second peptide substrate comprises a cleavable linkage (for cleavage by one or more mammalian proteases), the second peptide substrate is a methionine residue immediately N-terminal to the cleavable linkage. does not include In some embodiments, where the second peptide substrate comprises a plurality of cleavable bonds, the second peptide substrate comprises a methionine residue immediately N-terminal to at least one cleavable bond of the plurality of cleavable bonds. does not include In some embodiments, where the second peptide substrate comprises a plurality of cleavable bonds, the second peptide substrate contains a methionine residue immediately N-terminal to each cleavable bond of the plurality of cleavable bonds. do not include. In some embodiments, the second peptide substrate is #279, #280, #282, #283, #298, #299, #302, #303, #305, #307, #308, # of column II of Table A. 349, #396, #397, #416, #417, #418, #458, #459, #460, #466, #481 and #482 (or any combination thereof) comprising an amino acid sequence selected from the group consisting of: I never do that.

In some embodiments of the present disclosure, the peptide substrate (or first peptide substrate, or second peptide substrate) does not comprise a sequence selected from SEQ ID NOs: 1-8 . In some embodiments, the peptide substrate (or first peptide substrate or second peptide substrate) does not include the sequence of SEQ ID NO: 1 . In some embodiments, the peptide substrate (or the first peptide substrate or the second peptide substrate) does not include the sequence of SEQ ID NO:2 . In some embodiments, the peptide substrate (or first peptide substrate or second peptide substrate) does not include the sequence of SEQ ID NO:3 . In some embodiments, the peptide substrate (or first peptide substrate or second peptide substrate) does not include the sequence of SEQ ID NO:4 . In some embodiments, the peptide substrate (or first peptide substrate or fifth peptide substrate) does not include the sequence of SEQ ID NO:2 . In some embodiments, the peptide substrate (or first peptide substrate or second peptide substrate) does not include the sequence of SEQ ID NO:6 . In some embodiments, the peptide substrate (or first peptide substrate or second peptide substrate) does not include the sequence of SEQ ID NO:7 . In some embodiments, the peptide substrate (or first peptide substrate or second peptide substrate) does not include the sequence of SEQ ID NO:8 . In some embodiments, the peptide substrate (or first peptide substrate, or second peptide substrate) is immediately N-terminal to the cleavable bond (contained therein) (for cleavage by one or more mammalian proteases). does not contain methionine residues). In some embodiments, the peptide substrate (or first peptide substrate, or second peptide substrate) does not include a methionine residue immediately N-terminal to one or more cleavable bonds (contained therein). In some embodiments, the peptide substrate (or first peptide substrate, or second peptide substrate) does not include a methionine residue immediately N-terminal to any cleavable linkage (contained therein). In some embodiments, the peptide substrate (or the first peptide substrate or the second peptide substrate) is #279, #280, #282, #283, #298, #299, #302, #303, #302, #303, #305, #307, #308, #349, #396, #397, #416, #417, #418, #458, #459, #460, #466, #481 and #482 (or any combination thereof) ) does not contain an amino acid sequence selected from the group consisting of

In some embodiments of the therapeutic agent (or activatable therapeutic agent, or non-natural activatable therapeutic agent), a sequence of 6 to 10 contiguous amino acids of the peptide substrate (eg, first peptide substrate, second peptide substrate, etc.) is in Table A. contains up to 4, up to 3, up to 2 or up to 1 amino acid substitution(s) relative to the corresponding sequence of 6 to 10 contiguous amino acids of the sequence set forth in column II or column III (or a subset thereof) of . In some embodiments, the sequence of 6 to 10 contiguous amino acids of the peptide substrate (e.g., first peptide substrate, second peptide substrate, etc.) is of the sequence set forth in column II or column III (or a subset thereof) of Table A. identical to the corresponding 6 to 10 contiguous amino acid sequence. In some embodiments, the sequence of 8 to 10 contiguous amino acids of the peptide substrate (e.g., first peptide substrate, second peptide substrate, etc.) is of the sequence set forth in column II or column III (or a subset thereof) of Table A. up to 3, up to 2 or up to 1 amino acid substitution(s) relative to the corresponding sequence of 8 to 10 contiguous amino acids. In some embodiments, the sequence of 8 to 10 contiguous amino acids of the peptide substrate (e.g., first peptide substrate, second peptide substrate, etc.) is of the sequence set forth in column II or column III (or a subset thereof) of Table A. identical to the corresponding 8-10 contiguous amino acid sequence. In some embodiments, the sequence of 8 contiguous amino acids of the peptide substrate (e.g., first peptide substrate, second peptide substrate, etc.) corresponds to a sequence set forth in column II or column III (or a subset thereof) of Table A. Include up to 3, up to 2 or up to 1 amino acid substitution(s) for a sequence of 8 contiguous amino acids. In some embodiments, the sequence of 8 contiguous amino acids of the peptide substrate (e.g., first peptide substrate, second peptide substrate, etc.) corresponds to a sequence set forth in column II or column III (or a subset thereof) of Table A. It is identical to the sequence of 8 contiguous amino acids. In some embodiments, the 9 contiguous amino acid sequence of the peptide substrate (e.g., first peptide substrate, second peptide substrate, etc.) corresponds to a sequence set forth in column II or column III (or a subset thereof) of Table A. Include up to 3, up to 2 or up to 1 amino acid substitution(s) for a sequence of 9 consecutive amino acids. In some embodiments, the 9 contiguous amino acid sequence of the peptide substrate (e.g., first peptide substrate, second peptide substrate, etc.) corresponds to a sequence set forth in column II or column III (or a subset thereof) of Table A. identical to the contiguous amino acid sequence of 9. In some embodiments, the 10 contiguous amino acid sequence of the peptide substrate (e.g., first peptide substrate, second peptide substrate, etc.) corresponds to a sequence set forth in column II or column III (or a subset thereof) of Table A. Include at most 3, at most 2 or at most 1 amino acid substitution(s) for a sequence of 10 contiguous amino acids. In some embodiments, the 10 contiguous amino acid sequence of the peptide substrate (e.g., first peptide substrate, second peptide substrate, etc.) corresponds to a sequence set forth in column II or column III (or a subset thereof) of Table A. It is identical to the sequence of 10 contiguous amino acids.

In some embodiments of the therapeutic agent (or activatable therapeutic agent, or non-natural activatable therapeutic agent), the release segment (RS) (or the first release segment (RS1), or the second release segment (RS2) is ( each independently ) a peptide substrate (or first peptide substrate, or second peptide substrate) for cleavage by mammalian proteases such as serine proteases, cysteine proteases, aspartate proteases, threonine proteases or metalloproteinases. The release segment (RS) (or the first release segment (RS1), or the second release segment (RS2) is ( each independently ) disintegrin and metalloproteinase domain containing protein 10 (ADAM10), disintegrin and metallop Rotenase domain-containing protein 12 (ADAM12), disintegrin and metalloproteinase domain-containing protein 15 (ADAM15), disintegrin and metalloproteinase domain-containing protein 17 (ADAM17), disintegrin and metalloproteinase domain containing protein 9 (ADAM9), disintegrin and metalloproteinase with thrombospondin motif 5 (ADAMTS5), cathepsin B, cathepsin D, cathepsin E, cathepsin K, cathepsin L, cathepsin S, fibroblast activation protein alpha, hepsin, kallikrein-2, kallikrein-4, kallikrein-3, prostate specific antigen (PSA), kallikrein-13, legumain, matrix metallopeptidase 1 ( MMP-1), matrix metallopeptidase 10 (MMP-10), matrix metallopeptidase 11 (MMP-11), matrix metallopeptidase 12 (MMP-12), matrix metallopeptidase 13 (MMP-13), Matrix Metallopeptidase 14 (MMP-14), Matrix Metallopeptidase 16 (MMP-16), Matrix Metallopeptidase 2 (MMP-2), Matrix Metallopeptidase tidase 3 (MMP-3), matrix metallopeptidase 7 (MMP-7), matrix metallopeptidase 8 (MMP-8), matrix metallopeptidase 9 (MMP-9), matrix metal Lopeptidase 4 (MMP-4), Matrix Metallopeptidase 5 (MMP-5), Matrix Metallopeptidase 6 (MMP-6), Matrix Metallopeptidase 15 (MMP-15), A mammal selected from the group consisting of neutrophil elastase, protease activated receptor 2 (PAR2), plasmin, prostacin, PSMA-FOLH1, membrane type serine protease 1 (MT-SP1), matriptase and u-plasminogen It may include a peptide substrate (or a first peptide substrate, or a second peptide substrate) for cleavage by an animal protease. The releasing segment (RS) (or the first emitting segment (RS1) or the second emitting segment (RS2) is ( independently ) matrix metallopeptidase 1 (MMP1) (as examples, without limitation, in Table 1(a)). Sequences listed are substrate sequences), matrix metallopeptidase 2 (MMP2) (by way of example without limitation, sequences listed in Table 1(b) are substrate sequences), matrix metallopeptidase 7 (MMP7) ( By way of example without limitation, sequences listed in Table 1(c) are substrate sequences), matrix metallopeptidase 9 (MMP9) (by way of example without limitation, sequences listed in Table 1(d) are substrate sequences) , matrix metallopeptidase 11 (MMP11) (for example, without limitation, the sequence listed in Table 1(e) is a substrate sequence), matrix metallopeptidase 14 (MMP14) (for example, without limitation, the table The sequence listed in 1(f) is a substrate sequence), urokinase-type plasminogen activator (uPA) (as an example without limitation, the sequence listed in Table 1(g) is a substrate sequence), legumain (limiting A mammalian protease selected from the group consisting of, without limitation, the sequence listed in Table 1(h) as an example thereof is a substrate sequence and matriptase (without limitation, the sequence listed in Table 1(i) as an example thereof is a substrate sequence) The release segment (RS) (or the first release segment (RS1), or the second release segment (RS2) may include a peptide substrate (or first peptide substrate, or second peptide substrate) for cleavage by ( independently ) may include a peptide substrate (or a first peptide substrate, or a second peptide substrate) for cleavage by a plurality of mammalian proteases Peptide substrates (or first peptide substrates) susceptible to cleavage by mammalian proteases substrate, or second peptide substrate) may be susceptible to cleavage by a plurality of mammalian proteases, including mammalian proteases Peptide substrates (or first peptide substrate, or second peptide substrate) susceptible to cleavage by a plurality of mammalian proteases 2 peptide substrate) can have up to 4, or up to 3, or up to 2, or up to 1 amino acid substitution(s) relative to the sequence shown in Table 1(j) . Peptide substrates (or first peptide substrates, or second peptide substrates) susceptible to cleavage by multiple mammalian proteases are at most 4, or at most 3, or at most 2, for the sequences shown in Table 1(j) , or up to one amino acid substitution(s). Peptide substrates (or first peptide substrates, or second peptide substrates) susceptible to cleavage by multiple mammalian proteases are at most 4, or at most 3, or at most 2, for the sequences shown in Table 1(j) , or up to one amino acid substitution(s). A peptide substrate (or first peptide substrate, or second peptide substrate) susceptible to cleavage by a plurality of mammalian proteases may comprise the sequence shown in Table 1(j) .

In some embodiments of the therapeutic agent (or activatable therapeutic agent, or non-natural activatable therapeutic agent) comprising a set of release segments, each release segment in the set is ( independently ) a serine protease, a cysteine protease, an aspartate protease, a threonine It may include a peptide substrate for cleavage by a protease or a mammalian protease such as a metalloproteinase. Each release segment in the set is ( independently ) disintegrin and metalloproteinase domain containing protein 10 (ADAM10), disintegrin and metalloproteinase domain containing protein 12 (ADAM12), disintegrin and metalloproteinase domain protein 15 (ADAM15) containing the first domain, protein 17 (ADAM17) containing disintegrin and metalloproteinase domains, protein 9 (ADAM9) containing disintegrin and metalloproteinase domains, disintegrin with thrombospondin motif 5 and metalloproteinase (ADAMTS5), cathepsin B, cathepsin D, cathepsin E, cathepsin K, cathepsin L, cathepsin S, fibroblast activation protein alpha, hepsin, kallikrein-2, kallikrein- 4, kallikrein-3, prostate specific antigen (PSA), kallikrein-13, legumain, matrix metallopeptidase 1 (MMP-1), matrix metallopeptidase 10 (MMP-10), Matrix Metallopeptidase 11 (MMP-11), Matrix Metallopeptidase 12 (MMP-12), Matrix Metallopeptidase 13 (MMP-13), Matrix Metallopeptidase 14 (MMP-14) ), matrix metallopeptidase 16 (MMP-16), matrix metallopeptidase 2 (MMP-2), matrix metallopeptidase 3 (MMP-3), matrix metallopeptidase 7 (MMP -7), matrix metallopeptidase 8 (MMP-8), matrix metallopeptidase 9 (MMP-9), matrix metallopeptidase 4 (MMP-4), matrix metallopeptidase 5 (MMP-5), matrix metallopeptidase 6 (MMP-6), matrix metallopeptidase 15 (MMP-15), neutrophil elastase, protease activated receptor 2 (PAR2), plasmin, prostar peptide substrates for different mammalian proteases selected ( independently ) from the group consisting of syn, PSMA-FOLH1, membrane type serine protease 1 (MT-SP1), matriptase and u-plasminogen. Each release segment in the set is ( independently ) matrix metallopeptidase 1 (MMP1) (by way of example, without limitation, the sequences listed in Table 1(a) are substrate sequences), matrix metallopeptidase 2 ( MMP2) (sequences listed in Table 1(b) as examples without limitation are substrate sequences), matrix metallopeptidase 7 (MMP7) (sequences listed in Table 1(c) as examples without limitation are substrate sequences) sequence), matrix metallopeptidase 9 (MMP9) (as an example without limitation, the sequence listed in Table 1(d) is a substrate sequence), matrix metallopeptidase 11 (MMP11) (without limitation Sequences listed in Table 1(e) as examples are substrate sequences), matrix metallopeptidase 14 (MMP14) (without limitation, sequences listed in Table 1(f) as examples are substrate sequences), urokinase type Plasminogen activator (uPA) (sequences listed in Table 1(g) as examples without limitation are substrate sequences), legumain (sequences listed in Table 1(h) as examples thereof are substrate sequences) ) and matriptase (as a non-limiting example of which the sequences listed in Table 1(i) are substrate sequences) for different mammalian proteases selected ( independently ). In some cases, at least one release segment (RS) of a set of release segments may ( independently ) comprise a peptide substrate for cleavage by a plurality of mammalian proteases. Peptide substrates susceptible to cleavage by multiple mammalian proteases may have up to 4, or up to 3, or up to 2, or up to 1 amino acid substitution(s) relative to the sequences shown in Table 1(j) . Peptide substrates susceptible to cleavage by multiple mammalian proteases may have up to 4, or up to 3, or up to 2, or up to 1 amino acid substitution(s) relative to the sequences shown in Table 1(j) . Peptide substrates susceptible to cleavage by multiple mammalian proteases may have up to 4, or up to 3, or up to 2, or up to 1 amino acid substitution(s) relative to the sequences shown in Table 1(j) . Peptide substrates susceptible to cleavage by multiple mammalian proteases can include the sequences shown in Table 1(j) . One of ordinary skill in the art will understand that the sequences presented in Tables 1(a)-1(j) can be alternatively cleaved by one or more other proteases having substrate specificities similar to those of the corresponding proteases identified in the corresponding Tables as capable of cleaving the sequence. It will be understood that cleavage can be done with or additionally.

Table 1(a). Exemplary Peptide Substrates for Cleavage by Matrix Metallopeptidase 1 (MMP1)

Table 1(b). Exemplary Peptide Substrates for Cleavage by Matrix Metallopeptidase 2 (MMP2)

Table 1(c). Exemplary Peptide Substrates for Cleavage by Matrix Metallopeptidase 7 (MMP7)

Table 1(d). Exemplary Peptide Substrates for Cleavage by Matrix Metallopeptidase 9 (MMP9)

Table 1(e). Exemplary Peptide Substrates for Cleavage by Matrix Metallopeptidase 11 (MMP11)

Table 1(f). Exemplary Peptide Substrates for Cleavage by Matrix Metallopeptidase 14 (MMP14)

Table 1(g). Exemplary Peptide Substrates for Cleavage by Urokinase-Type Plasminogen Activator (uPA)

Table 1(h). Exemplary Peptide Substrates for Cleavage by Legumain

Table 1(i). Exemplary Peptide Substrates for Cleavage by Matriptase

Table 1(j). Exemplary Peptide Substrates for Cleavage by Multiple Proteases

Masking Moiety (MM)

A masking moiety (MM) of the present disclosure can specifically or It can interact non-specifically, masking the BM by inhibiting or reducing (at least in certain cases) the ability of the BM to bind to the designated target(s). In some instances, a masking moiety (MM) can specifically bind to or have a specific affinity for a biologically active moiety (e.g., an antibody or antibody fragment), thereby allowing the designed target (e.g., may interfere with and/or inhibit binding of the BM to the antigenic target). In some cases, the masking moiety does not have significant affinity for the biologically active moiety, but exerts a masking effect due to non-specific steric hindrance.

In some embodiments of the therapeutic agent (or activatable therapeutic agent, or non-natural activatable therapeutic agent), the masking moiety (MM) (or first masking moiety (MM1), or second masking moiety (MM2)) comprises: ( each independently, individually or collectively ) when linked to a corresponding therapeutic agent, a biologically active moiety directed against a target tissue or cell (such as those described in the Target Tissue or Cell section below or elsewhere herein) may interfere with the interaction of BM, resulting in target cell markers carried by the target tissue or cell when the therapeutic is in an uncut state (e.g., described in the Target Tissue or Cell section below or described herein). described elsewhere) and the dissociation constant (Kd) of the BM of the therapeutic is the dissociation constant (Kd) of the target cell marker and the corresponding biologically active moiety (remaining after the releasing segment (RS) is cleaved and the MM is released) _d ) may be larger compared to When the therapeutic agent is in an uncleaved state, the dissociation constant (K _d ) of the target cell marker and the biologically active moiety (BM) of the therapeutic agent is at least (about ) 2 times, at least (about) 5 times, at least (about) 10 times, at least (about) 50 times, at least (about) 100 times, at least (about) 200 times, at least (about) 300 times, at least (about) 400 times, at least (about) 500 times, at least (about) 600 times, at least (about) 700 times, at least (about) 800 times, at least (about) 900 times, or at least (about) 1000 times. The dissociation constant (Kd) can be determined in an in vitro assay under equimolar concentrations. In vitro assays include cell membrane integrity assay, mixed cell culture assay, cell-based competitive binding assay, FACS-based propidium iodide assay, trypan blue influx assay, photometric enzyme release assay, radiometric 51Cr release assay, fluorescence assay europium release assay, CalceinAM release assay, photometric MTT assay, XTT assay, WST-1 assay, Alamar blue assay, radiometric 3H-Thd incorporation assay, clonogenic assay to measure cell division activity, fluorescence to measure mitochondrial transmembrane gradients Rhodamine 123 assay, FACS-based apoptosis assay monitored by phosphatidylserine exposure, ELISA-based TUNEL test assay, sandwich ELISA, caspase activity assay, cell-based LDH release assay and cell morphology assay, reporter gene activity assay, or both can be selected from any combination.

In some embodiments of a therapeutic agent (or an activatable therapeutic agent, or a non-natural activatable therapeutic agent), the therapeutic agent may result in an enhanced safety profile. For example, compared to the corresponding biologically active moiety (which remains after the release segment (RS) is cleaved and the MM is released), improving the maximum tolerated exposure level (MTEL) and/or target tissue or cell (e.g., side effects (eg, cytotoxicity) in the delivery of BM to a target tissue or cell section below or as described elsewhere herein) may be reduced. A therapeutic agent in which a biologically active moiety (BM) is linked (directly or indirectly) to a masking moiety (MM) (or a first masking moiety (MM1), or a second masking moiety (MM2)) has a safety profile of can lead to enhancement. For example, at least (about) 2-fold, at least (about) 5-fold, at least ( adverse effects (e.g. For example, cytotoxicity) can be reduced.

In some embodiments of a therapeutic agent (or an activatable therapeutic agent, or a non-natural activatable therapeutic agent), the therapeutic agent may have a longer elimination half-life compared to the corresponding biologically active moiety. A therapeutic agent in which a biologically active moiety (BM) is linked (directly or indirectly) to a masking moiety (MM) (or a first masking moiety (MM1), or a second masking moiety (MM2)) has a corresponding biological at least (about) 2 times, at least (about) 5 times, at least (about) 10 times, at least (about) 15 times, at least (about) 20 times, at least (about) 50 times the elimination half-life of the active moiety, or It may have an elimination half-life that is at least (about) 100 times longer.

In some embodiments, a therapeutic agent may be less immunogenic compared to the corresponding biologically active moiety. A therapeutic agent in which a biologically active moiety (BM) is linked (directly or indirectly) to a masking moiety (MM) (or a first masking moiety (MM1), or a second masking moiety (MM2)) has a corresponding biological may be at least (about) 2-fold, at least (about) 5-fold, or at least (about) 10-fold less immunogenic than the active moiety. Immunogenicity can be determined by measuring the production of IgG antibodies that selectively bind to biologically active moieties following administration of similar doses to a subject.

In some embodiments, a therapeutic agent may have a higher apparent molecular weight factor under physiological conditions compared to the corresponding biologically active moiety. A therapeutic agent in which a biologically active moiety (BM) is linked (directly or indirectly) to a masking moiety (MM) (or a first masking moiety (MM1), or a second masking moiety (MM2)) has a corresponding biological at least (about) 1.5-fold, at least (about) 2-fold, at least (about) 5-fold, at least (about) 8-fold, at least (about) 10-fold, at least (about) 12-fold, at least It may have an apparent molecular weight factor that is (about) 15 times, at least (about) 18 times, or at least (about) 20 times greater.

In some embodiments of a therapeutic agent (or an activatable therapeutic agent, or a non-natural activatable therapeutic agent) comprising a first masking moiety (MM1) and a second masking moiety (MM2), both MM1 and MM2 are linked to the therapeutic agent. when ( each independently, individually or collectively ) of a biologically active moiety (BM) to a target tissue or cell (e.g., described in the Target Tissue or Cell section below or elsewhere herein). interaction, resulting in target cell markers carried by the target tissue or cell when the therapeutic agent is in an uncut state (e.g., described in the Target Tissue or Cell section below or described elsewhere herein). the biologically active moiety (BM) of the therapeutic agent) and the biologically active peptide (one or both of the release segment (RS1) and the second release segment (RS2) are cleaved and the dissociation constant (K _d ) of the biologically active moiety (BM) of the therapeutic agent corresponds to MM1 and MM2 may be greater compared to the dissociation constant (Kd) of one or both of which remain after being released. When the therapeutic agent is in its uncleaved state, the dissociation constant (Kd) of the target cell marker and the biologically active moiety (BM) of the therapeutic agent is at least (about) twice, at least ( About) 5 times, at least (about) 10 times, at least (about) 50 times, at least (about) 100 times, at least (about) 200 times, at least (about) 300 times, at least (about) 400 times, at least (about) ) 500 times, at least (about) 600 times, at least (about) 700 times, at least (about) 800 times, at least (about) 900 times, or at least (about) 1000 times. The dissociation constant (Kd) can be determined in an in vitro assay under equimolar concentrations. In vitro assays include cell membrane integrity assay, mixed cell culture assay, cell-based competitive binding assay, FACS-based propidium iodide assay, trypan blue influx assay, photometric enzyme release assay, radiometric ⁵¹ Cr release assay, fluorescence assay Europium release assay , Calcein AM release assay, photometric MTT assay, XTT assay, WST-1 assay, Alamar blue assay, radiometric assay, 3H-Thd incorporation assay, clonogenic assay to measure cell division activity, mitochondrial transmembrane gradient Fluorescence rhodamine 123 assay, FACS-based apoptosis assay monitored by phosphatidylserine exposure, ELISA-based TUNEL test assay, sandwich ELISA, caspase activity assay, cell-based LDH release assay, reporter gene activity assay, and cell morphology assay; or any combination thereof.

In some embodiments of the therapeutic agent (or activatable therapeutic agent, or non-natural activatable therapeutic agent) comprising a first masking moiety (MM1) and a second masking moiety (MM2), the biologically active moiety (BM) is MM1 and MM2, either directly or indirectly, may result in an enhanced safety profile. For example, compared to the corresponding biologically active moiety (which remains after one or both of the release segment (RS1) and the second release segment (RS2) is cleaved and one or both of MM1 and MM2 is released) , improve maximum tolerated exposure levels (MTEL) and/or reduce side effects (eg, cytotoxicity) in the delivery of biologically active moieties (BMs) to target tissues or cells. A therapeutic agent in which the biologically active moiety (BM) is linked (directly or indirectly) to one or both of MM1 and MM2 may result in an enhanced safety profile. For example, at least (about) 2-fold, at least (about) 5-fold, at least ( adverse effects (e.g. For example, cytotoxicity) can be reduced.

In some embodiments of the therapeutic agent (or activatable therapeutic agent, or non-natural activatable therapeutic agent) comprising a first masking moiety (MM1) and a second masking moiety (MM2), the biologically active moiety (BM) is MM1 and MM2 is directly or indirectly linked to one or both of the corresponding biologically active moieties (one or both of the release segment (RS1) and the second release segment (RS2) are cleaved and one of MM1 and MM2 or both remain after release), may have a longer elimination half-life. A therapeutic agent in which a biologically active moiety (BM) is linked (directly or indirectly) to one or both of MM1 and MM2 has an elimination half-life of at least (about) 2 times, at least (about) 5 times the corresponding biologically active moiety. times, at least (about) 10 times, at least (about) 15 times, at least (about) 20 times, at least (about) 50 times, at least (about) 100 times longer.

In some embodiments of the therapeutic agent (or activatable therapeutic agent, or non-natural activatable therapeutic agent) comprising a first masking moiety (MM1) and a second masking moiety (MM2), the biologically active moiety (BM) is MM1 and MM2 is directly or indirectly linked to one or both of the corresponding biologically active moieties (one or both of the release segment (RS1) and the second release segment (RS2) are cleaved and one of MM1 and MM2 or both remain after being released), may be less immunogenic. A therapeutic agent in which a biologically active moiety (BM) is linked (directly or indirectly) to one or both of MM1 and MM2 is at least (about) 2-fold, at least (about) 5-fold, or It may be at least (about) 10 times less immunogenic. Immunogenicity can be determined by measuring the production of IgG antibodies that selectively bind to biologically active moieties following administration of similar doses to a subject.

In some embodiments of the therapeutic agent (or activatable therapeutic agent, or non-natural activatable therapeutic agent) comprising a first masking moiety (MM1) and a second masking moiety (MM2), the biologically active moiety (BM) is MM1 and MM2 may have a greater apparent molecular weight factor under physiological conditions compared to the corresponding biologically active moiety. A therapeutic agent in which a biologically active moiety (BM) is linked (directly or indirectly) to one or both of MM1 and MM2 is at least (about) 1.5 times, at least (about) 2 times more effective under physiological conditions than the corresponding biologically active moiety. times, at least (about) 5 times, at least (about) 8 times, at least (about) 10 times, at least (about) 12 times, at least (about) 15 times, at least (about) 18 times, or at least (about) 20 times. can have an apparent molecular weight factor that is twice as large.

In some embodiments of the therapeutic agent (or activatable therapeutic agent, or non-natural activatable therapeutic agent), the masking moiety (MM) (or first masking moiety (MM1), or second masking moiety (MM2)) is ( each independently ) extended recombinant polypeptide (XTEN). XTENs can be characterized as: (i) contain at least 100 amino acids; (ii) at least 90% of the amino acid residues are selected from glycine (G), alanine (A), serine (S), threonine (T), glutamate (E) and proline (P); (iii) at least four different types of amino acids selected from G, A, S, T, E and P. XTENs can be characterized as: (i) contain at least 150 amino acids; (ii) at least 90% of the amino acid residues are selected from glycine (G), alanine (A), serine (S), threonine (T), glutamate (E) and proline (P); (iii) at least four different types of amino acids selected from G, A, S, T, E and P. The extended recombinant polypeptide (XTEN) is ( each independently ) at least (about) 90%, at least (about) 91%, at least (about) 92%, at least (about) 93%, at least (about) 94%, at least (about) 95%, at least (about) 96%, at least (about) 97%, at least (about) 98%, at least (about) 99%, or 100 It may include amino acid sequences with % sequence identity.

(1) a first masking moiety (MM1) comprising a first extended recombinant polypeptide (XTEN1) and (2) a second masking moiety (MM2) comprising a second extended recombinant polypeptide (XTEN2). In some embodiments of the therapeutic agent (or activatable therapeutic agent, or non-natural activatable therapeutic agent), XTEN2 may be characterized as follows: (i) comprises at least 100 amino acids; (ii) at least 90% of the amino acid residues are selected from glycine (G), alanine (A), serine (S), threonine (T), glutamate (E) and proline (P); (iii) at least four different types of amino acids selected from G, A, S, T, E and P. XTEN2 can be characterized as: (i) comprises at least 150 amino acids; (ii) at least 90% of the amino acid residues are selected from glycine (G), alanine (A), serine (S), threonine (T), glutamate (E) and proline (P); (iii) at least four different types of amino acids selected from G, A, S, T, E and P. XTEN2 is at least ( about ) 90%, at least (about) 91%, at least (about) 92%, at least (about) 93%, At least (about) 94%, at least (about) 95%, at least (about) 96%, at least (about) 97%, at least (about) 98%, at least (about) 99%, or 100% sequence identity. It may contain an amino acid sequence.

In some embodiments, XTEN (or XTEN1, or XTEN2) can ( each independently ) comprise or be formed from ( each independently ) a plurality of non-overlapping sequence motifs. At least one of the non-overlapping sequence motifs may be repetitive (or may be repeated at least twice in the corresponding XTEN). At least one of the non-overlapping sequence motifs may be non-repetitive (or may be found only once within the corresponding XTEN). A plurality of non-overlapping sequence motifs are (i) a set of non-overlapping sequence motifs in which each motif in the set is repeated (repeated) at least twice in the corresponding XTEN and (ii) occurs (or is found only once) in the corresponding XTEN. ) non-overlapping (non-repeating) sequence motifs. Each non-overlapping sequence motif may be 9 to 14 (or 10 to 14, or 11 to 13) amino acids in length. Each non-overlapping sequence motif can be 12 amino acids in length. The plurality of non-overlapping sequence motifs may comprise a set of non-overlapping (repeated) sequence motifs, wherein each motif in the set (1) may be repeated at least twice in the corresponding XTEN and (2) contain between 9 and 14 It can be an amino acid length. (Repetition) The set of non-overlapping sequence motifs may include a 12-mer sequence motif selected from the group shown in Table 2a . (Repetition) The set of non-overlapping sequence motifs may include a 12-mer sequence motif selected from the group shown in Table 2a . (Repetition) The set of non-overlapping sequence motifs may include at least 2, at least 3 or all 4 of the 12-mer sequence motifs in the groups shown in Table 2a .

Table 2a. Exemplary 12-mer Sequence Motifs for XTEN Construction

* Represents individual motif sequences that when used together in various permutations create a "family sequence"

Table 2b. Exemplary XTEN Polypeptides

Table 2c. Exemplary XTEN Polypeptides

Additional examples of XTEN sequences that can be used in accordance with the present disclosure are described in US Patent Publication Nos. 2010/0239554 A1, 2010/0323956 A1, 2011/0046060 A1, 2011/0046061 A1, 2011/0077199 A1, 2011/0172146 A1, 2018/ 0244736 A1, 2018/0346952 A1 and 2019/0153115 A1; U.S. Patent Nos. 8,673,860, 9,371,369, 9,926,351, 9,249,211 and 9,976,166; and International Patent Publication Nos. WO 2010/091122 A1, WO 2010/144502 A2, WO 2010/144508 A1, WO 2011/028228 A1, WO 2011/028229 A1, WO 2011/028344 A2, WO 2014/011819 A2, WO 2015/ 023891, WO 2016/077505 A2, WO 2017/040344 A2 and WO 2019/126576 A1.

Generally, an XTEN is a polypeptide having a non-naturally occurring, substantially non-repetitive sequence with or without a low degree of secondary or tertiary structure under physiological conditions and the additional characteristics described in the following paragraphs. XTEN is at least (about) 100, at least (about) 150, at least (about) 200, at least (about) 300, at least (about) 400, at least (about) 500, at least (about) 600, at least (about) 700, at least (about) 800, at least (about) 900, at least (about) 1,000 amino acids, or a range in between any of the foregoing. As used herein, XTEN specifically excludes whole antibodies or antibody fragments (eg, single chain antibodies and Fc fragments). XTEN polypeptides have utility as fusion partners in that they serve a variety of roles conferring certain desirable properties, for example, when linked to a composition comprising one or more biologically active moieties (eg, those described herein). The resulting composition has enhanced properties, such as enhanced pharmacokinetics, physicochemical, pharmacological and improved toxicological and pharmaceutical properties compared to the corresponding one or more biologically active moieties not linked to XTEN, which properties combine them into one The use of any of the above biologically active moieties makes them useful in the treatment of certain conditions known in the art.

The unstructured nature and physicochemical properties of XTEN are in part due to the overall amino acid composition disproportionately limited to four to six types of hydrophilic amino acids, the sequence of amino acids of a quantifiable, substantially non-repetitive design, and thus the length of the XTEN polypeptide. arises from In an advantageous feature common to XTEN but not common to natural polypeptides, the properties of the XTENs disclosed herein have similar properties within a range of lengths, as evidenced by the diversity of exemplary sequences in Tables 2b-2c , and compositions in which they are ligated. may not be related to the absolute primary amino acid sequence that imparts enhanced properties, many of which are documented in the Examples. Indeed, compositions of the present disclosure are not limited to the XTENs specifically listed in Tables 8 or 10; instead, the present embodiments exhibit the properties of the XTENs described herein, when optimally aligned, in Tables 2b-2c. It is specifically contemplated to include sequences that have at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to the sequence of . It has been established that these XTENs have properties more similar to non-proteinaceous, hydrophilic polymers (eg, polyethylene glycol or "PEG") than proteins. XTENs of the present disclosure exhibit one or more of the following advantageous properties: defined constant length (for a given sequence), conformational flexibility, reduced or lack of secondary structure, highly random coil formation, highly water solubility, highly protease resistance, low immunogenicity, low binding to mammalian receptors, a defined degree of charge and increased hydrodynamic (or Stokes) radius; Similar properties to certain hydrophilic polymers (eg, polyethylene glycol) that make them particularly useful as fusion partners.

As described herein, XTEN is designed to behave like a denatured peptide sequence under physiological conditions despite the extended length of the polymer. "Denatured" describes a state of a peptide in solution characterized by great conformational freedom of the peptide backbone. Most peptides and proteins are denatured in the presence of high concentrations of denaturants or at high temperatures. The denatured form of the peptide, for example, has a characteristic circular dichroism (CD) spectrum and is characterized by a lack of long-range interactions as determined by NMR. “Modified form” and “unstructured form” are used synonymously herein. In some embodiments, the present disclosure provides a composition comprising a denatured sequence substantially free of secondary structure under physiological conditions and an XTEN sequence similar under physiological conditions. As used in this context, "substantially free" means that at least about 80%, or about 90%, or about 95%, or about 97%, or at least about 99% of the XTEN amino acid residues of the XTEN sequence are subject to algorithmic or spectrophotometric analysis. does not contribute to secondary structure when measured or determined by the methods described herein, including

A variety of well-established methods and assays are known in the art for determining and confirming the physicochemical properties of subject XTENs and subject polypeptide compositions into which they are incorporated. These properties include, but are not limited to, secondary or tertiary structure, solubility, protein aggregation, stability, absolute and apparent molecular weight, purity and uniformity, melting properties, contamination and moisture content. Methods for measuring these properties include analytical centrifugation, EPR, HPLC-ion exchange, HPLC-size exclusion chromatography (SEC), HPLC-reverse phase, light scattering, capillary electrophoresis, circular dichroism, differential scanning calorimetry, fluorescence These include luminescence, HPLC-ion exchange, HPLC-size exclusion, IR, NMR, Raman spectroscopy, refraction and UV/visible spectroscopy. In particular, the secondary structure can be measured spectrophotometrically, for example by circular dichroism spectroscopy in the "far-UV" spectral region (190-250 nm). Secondary structural components, such as alpha helices and beta sheets, each give rise to the characteristic shape and magnitude of the CD spectrum due to the lack of these structural components. Secondary structures can also be determined by certain computer programs or algorithms, such as the well-known Chou-Fasman algorithm (Chou, PY, et al. (1974) Biochemistry , 13: 222-45), as described in US Patent Application No. 20030228309A1. ]) and the Garnier-Osguthorpe-Robson algorithm ("GOR IV algorithm") (Garnier J, Gibrat JF, Robson B. (1996), GOR method for predicting protein secondary structure from amino acid sequence. Methods Enzymol 266:540- 553]) can predict the polypeptide sequence. For a given sequence, an algorithm can predict whether some or no secondary structure is present, for example, as the total number of residues in the sequence that form an alpha helix or beta sheet and/or as a percentage thereof, or as a random number. Expressed as the percentage of sequence residues predicted to cause coil formation (lack of secondary structure). Polypeptide sequences can be obtained by the Chou-Fasman algorithm using, for example, the site on the World Wide Web at fasta.bioch.virginia.edu/fasta_www2/fasta_www.cgi?rm=misc1 and npsa-pbil.ibcp.fr/cgi-bin/ This can be analyzed using the GOR IV algorithm at npsa_automat.pl?page=npsa_gor4.html (both sites accessed 12/08/2017). Random coils use intrinsic viscosity measurements to tune chain length in a conformation-dependent manner (Tanford, C., Kawahara, K. & Lapanje, S. (1966) J. Biol. Chem. 241, 1921-1923). ), as well as size exclusion chromatography (Squire, PG, Calculation of hydrodynamic parameters of random coil polymers from size exclusion chromatography and comparison with parameters by conventional methods. Journal of Chromatography, 1981, 5,433-442). method can be determined. Additional methods are described in Arnau, et al. , Prot Expr and Purif (2006) 48, 1-13.

In some embodiments of the present disclosure, the activatable therapeutic agent is an activatable antibody (AA) composition, wherein a masking moiety (MM) is coupled to an antibody or antibody fragment (AB) and an antigen binding domain of the AB (e.g. Refers to an amino acid sequence positioned to reduce the ability of an AB to bind to a designated binding target, eg, by specifically binding to a complementarity determining region(s) (CDR(s)). Such binding may be non-covalent. In some embodiments, the activatable antibody composition can prevent binding of the designated binding target by binding the MM to the N- or C-terminus of the activatable antibody composition.

Alternatively, the MM may not specifically bind to the AB but rather interfere with AB target binding through non-specific interactions such as steric hindrance. For example, a MM can be modified so that the tertiary or quaternary structure of the activatable antibody is uncleaved to hold the MM in place, allowing the MM to mask the AB through charge-based interactions, thereby hindering target access to the AB. activatable antibody composition. The masking moiety (MM) can allosterically or sterically hinder and/or inhibit binding of the antibody or antibody fragment (AB) to the target.

When an antibody or antibody fragment (AB) is modified with MM and the target is present, the specific binding of the AB to the target may be reduced or inhibited compared to the specific binding of the AB that is not modified with MM to the target. The dissociation constant (K _d ) of an AB modified with MM to its target will generally be greater than the corresponding K _d of an AB not modified with MM to its target. Conversely, the binding affinity of an AB modified with MM to its target may generally be lower than that of an AB not modified with MM to its target. In some embodiments, the masking moiety (MM) of the activatable antibody composition is an antibody or fragment greater than the equilibrium dissociation constant of the antibody or fragment thereof for binding to a designated binding target (near or at a diseased site of a subject). It may have an equilibrium dissociation constant (K _d ) for binding to its fragments.

When an antibody or antibody fragment (AB) is modified with a releasing segment (RS) and a masking moiety (MM) and the target is present but there is no protease or protease activity sufficient to cleave the RS, specificity of the modified AB to the target Binding may generally be reduced or inhibited compared to the specific binding of AB modified with RS and MM in the presence of a protease or protease activity sufficient to cleave the target and RS. For example, where the modified antibody is an activatable antibody composition and comprises a release segment (RS), the AB can be unmasked upon cleavage of the RS in the presence of a protease, preferably a disease specific protease. Thus, a MM provides masking of the AB from target binding when the activatable antibody composition is uncleaved, but substantially or significantly interferes with or competes for binding of the target to the AB when the activatable antibody composition is present in a truncated form. It is not. A schematic diagram of an exemplary activatable antibody (AA) composition is provided in FIG. 3 . As illustrated, the release segment (RS) binds the antibody or antibody fragment (AB) to the target in the cleaved (or relatively active state) and in the presence of the target, but in the uncleaved (or relatively inactive state) is positioned such that, in the presence of the target, specific binding of the AB to the target is reduced or inhibited. The specific binding of an antibody or antibody fragment (AB) to a target may be reduced due to inhibition or masking of the ability of the AB to specifically bind to the target by the masking moiety (MM).

In some embodiments of the activatable antibody composition, where the antibody or antibody fragment (AB) is capable of specifically binding to a designated binding target, coupling of the masking moiety (MM) to the antibody or antibody fragment (AB) is Reduce the ability of the AB to bind the designated binding target compared to the ability of the AB not coupled to the MM to bind the designated binding target (eg, when assayed in vitro using a target displacement assay) . This coupling of the MM to the AB can reduce the ability of the AB to bind to its designated binding target over a period of time.

The masking moiety (MM) can be provided in a variety of different forms. In certain embodiments, a MM can be selected to be a known binding partner of an antibody or antibody fragment (AB), provided that the MM is selected after cleavage of the releasing segment (RS) to reduce interference of the MM in target-AB binding. The AB binds with a lower affinity and/or avidity than the target protein it is designed to bind to. In other words, as discussed above, the MM masks the AB from target binding when the activatable antibody composition is uncleaved, but substantially or significantly prevents binding to the target when the activatable antibody composition is present in a truncated conformation. or not compete for it. In certain embodiments, AB and MM do not contain the amino acid sequence of a naturally occurring binding partner pair, such that at least one of AB and MM does not have the amino acid sequence of a member of a naturally occurring binding partner. The masking moiety (MM) may not contain more than 50% amino acid sequence identity with the natural binding partner of the antibody or antibody fragment (AB). A masking moiety (MM) may comprise a consensus sequence specific for binding to a class of antibodies for a designated binding target (eg, a diseased target). A MM can be a polypeptide that is less than 40 amino acids in length (eg, 2 to 40). The MM can be covalently coupled to the activatable antibody composition.

In some embodiments, the present disclosure provides an activatable antibody complex (AAC) composition (as shown in FIG. 4 ) comprising: (1) 2 components, each capable of specifically binding to a designated binding target; an antibody or antibody fragment (AB1 and AB2), (2) at least one masking moiety coupled to AB1 or AB2 and capable of inhibiting the specific binding of AB1 and AB2 to the designated binding target(s) (MM ) and (3) at least one release segment (RS) coupled to AB1 or AB2 and capable of being specifically cleaved by a protease to activate the AAC composition. In some embodiments, when the AAC is in an uncleaved state, the MM is capable of inhibiting specific binding of AB1 and AB2 to the designated binding target(s), and when the AAC is in a cleaved state, the MM is capable of inhibiting the specific binding of AB1 and AB2 to the designated binding target(s). It does not inhibit the specific binding of AB1 and AB2 to the binding target. The two ABs may bind to different targets or to different epitopes of the same target.

In some embodiments, the MM does not inhibit cell entry of the activatable antibody composition.

In some embodiments, the masking moiety (MM) may include an anti-albumin domain, such as a single domain antibody (sdAb) anti-albumin domain. In some embodiments, an anti-albumin domain may comprise non-CDR loops, CDR loops, or any combination thereof. In some embodiments, an anti-albumin domain may include non-CDR loops and CDR loops. A non-CDR loop is capable of binding one or more antibodies or antibody fragments (AB) (eg, but not limited to, CDRs of an AB) of an activatable antibody (AA) composition, thereby binding to the designated target(s). An AB can be masked (at least in some cases) by suppressing or reducing its ability. The CDR loops are capable of binding albumin (eg, human serum albumin) such that (at least in some cases) an AB in an activatable antibody (AA) composition binds to the designated target(s) via steric or allosteric hindrance. masking and/or imparting half-life extension to the AA composition. In some embodiments, non-CDR loops can be engineered into different positions of the anti-albumin sdAb domain. In some embodiments, the MM has (1) (1a) specific binding to the target recognition region of the AB and/or (1b) the ability of the AB to bind to designated target(s) through steric masking of the target recognition region of the AB. and/or MM can (2) confer half-life extension to AA, including AB, through binding to albumin. The MM may be covalently coupled (directly or indirectly) to the activatable antibody composition.

As illustrated in the schematic diagram shown in FIG. 5 , an exemplary activatable antibody complex (AAC) composition can include: (1) at least two components, each capable of specifically binding to designated binding target(s); an antibody or antibody fragment (AB1 and AB2), (2) at least one masking moiety coupled to AB1 or AB2 and capable of inhibiting specific binding of AB1 or AB2 to the designated binding target(s) (MM ) and (3) at least one release segment (RS) coupled to AB1 or AB2 and capable of being specifically cleaved by a protease to activate the activatable antibody complex (AAC) composition. In some embodiments, when AA is in an uncleaved state, the MM is capable of inhibiting specific binding of AB1 or AB2 to the designated binding target(s), and the activatable antibody complex (AAC) composition is in a cleaved state. When present, MM does not inhibit specific binding of AB1 or AB2 to the designated binding target(s). In some embodiments, the masking moiety (MM) can be coupled to AB1 and AB2 via two separate emissive segments (RS). That is, the MM may be coupled to the C-terminus of AB1 and the N-terminus of AB2, or may be coupled to the N-terminus of AB1 and the C-terminus of AB2 and positioned between AB1 and AB2.

In some embodiments of the present disclosure, the activatable therapeutic agent is an activatable antibody (AA) composition, wherein the masking moiety (MM) refers to an amino acid sequence coupled to an antibody or antibody fragment (AB) (e.g. , scFv, sdAb, or fragment thereof), positioned to reduce the ability of the AB to dimerize with other antibodies or antibody fragments, thereby preventing the formation of antibodies or antibody fragments capable of binding to the target. Such binding may be non-covalent. In some embodiments, the activatable antibody composition can prevent binding of the designated binding target by binding the MM to the N- or C-terminus of the activatable antibody composition.

When an antibody or antibody fragment (AB) is modified with MM and the target is present, the specific binding of the AB to its dimerization partner is reduced or inhibited compared to the specific binding of an AB not modified with MM to its dimerization partner It can be. The dissociation constant (K _d ) of an AB modified with MM to its dimerization partner will generally be greater than the corresponding K _d of an AB not modified with MM to its dimerization partner. Conversely, the binding affinity of an AB modified with MM to its dimerization partner may generally be lower than that of an AB not modified with MM to its dimerization partner. In some embodiments, the masking moiety (MM) of the activatable antibody composition has an equilibrium dissociation constant for binding of the antibody or fragment thereof that is greater than the equilibrium dissociation constant of the antibody or fragment thereof for binding to the designated dimerization partner ( K _d ).

When an antibody or antibody fragment (AB) is modified with a releasing segment (RS) and a masking moiety (MM) and the target is present but there is no protease or protease activity sufficient to cleave the RS, it dimerizes with another antibody or antibody fragment. The specific ability of the modified AB and thus the ability of the dimer to bind to the designated binding target(s) is dependent on the specificity of the AB modified with RS and MM in the presence of a protease or protease activity sufficient to cleave the target and RS. Compared to the ability of dimerization and the subsequent ability of the dimer to bind to the designated binding target(s), it may generally be reduced or inhibited. For example, where the modified antibody is an activatable antibody composition and comprises a release segment (RS), the AB can be unmasked upon cleavage of the RS in the presence of a protease, preferably a disease specific protease. Thus, a MM provides for masking of an AB from dimerization with another AB when the activatable antibody composition is not cleaved, and for reducing or inhibiting the binding of the resulting dimer to its designated binding target(s), but not for activatable antibody composition. When the composition is present in truncated form, it does not substantially or significantly prevent or compete for dimerization to another AB and the reduction or inhibition of binding of the resulting dimer to its designated binding target(s).

Masking moieties can be provided in different forms. In some embodiments, the masking domain can be an inhibitory antibody or antibody fragment (IAB; eg, but not limited to, a VL or VH domain), provided that the MM reduces interference of the MM in AB-AB dimerization. After cleavage of the release segment (RS) to allow the AB to dimerize, it binds to the AB with lower affinity and/or avidity than the dimerization partner it was designed to dimerize. In other words, as discussed above, a MM masks an AB from dimerization to another AB when the activatable antibody composition is uncleaved, but dimerizes with another AB when the activatable antibody composition is present in a truncated conformation. does not substantially or substantially interfere with, or compete with, The MM can be covalently coupled to the activatable antibody composition.

In some embodiments, the present disclosure provides an activatable antibody complex (AAC) composition (as shown in FIG. 6 ) comprising: (1) two antibodies or antibody fragments (AB1 and AB2) (2 ) two masking moieties (MM), each coupled to AB1 and AB2, capable of reducing or inhibiting the specific dimerization of AB1 and AB2 and subsequent binding of the AB1-AB2 complex to the designated binding target(s); , (3) at least three release segments (RS) coupled to AB1, AB2 and MM and capable of being specifically cleaved by a protease to activate the AAC composition, (4) coupled to AB1 and/or AB2 at least one additional antibody or antibody fragment (AB3 and/or AB4; eg, but not limited to scFv or sdAb). In some embodiments, when the AAC is in an uncleaved state, the MM is capable of inhibiting or reducing the specific dimerization of AB1 and AB2, followed by binding of the resulting AB1-AB2 dimers to their designated binding target(s). When AAC is in a cleaved state, MM reduces or does not inhibit specific dimerization of AB1 and AB2 and subsequent binding of AB1-AB2 dimers to their designated binding target(s). It does not reduce or inhibit binding. When more than one additional AB is coupled to AB1 and/or AB2, the additional ABs may bind the same target or different targets.

In some embodiments, the MM is a coiled-coil domain, e.g., (1) a high affinity parallel heterodimer leucine zipper coiled-coil domain containing or lacking cysteine, (2) containing or containing cysteine. low affinity parallel heterodimeric twisted-coil leucine zipper domain, (3) disulfide linkage covalent twisted-coil domain, (4) anti-parallel heterodimeric leucine zipper twisted-coil domain, (5) helix-turn-helix homodimer leucine zipper It may include (but is not limited to) twisted coil domains. The MM may be covalently coupled (directly or indirectly) to the activatable antibody composition. In some embodiments, the MM may reduce or inhibit binding of the AB to its intended target(s) through steric or allosteric hindrance.

In some embodiments, the present disclosure provides an activatable antibody complex (AAC) composition (as shown in FIG. 7 ) comprising: (1) at least one antibody or antibody fragment (AB), (2) ) at least one masking moiety (MM) coupled to the AB and capable of inhibiting the specific binding of the AB to the designated binding target, and (3) coupled to the AB and specifically cleaved by a protease to form an AAC At least one release segment (RS) capable of activating the composition. In some embodiments, when the AAC is in an uncleaved state, the MM is capable of reducing or inhibiting specific binding of the AB to the designated binding target(s), and when the AAC is in a cleaved state, the MM is capable of It does not reduce or inhibit the specific binding of the AB to its designated binding target(s).

In some embodiments, an activatable therapeutic agent may comprise a cleavage sequence described herein and/or is likely to be a responder to a therapeutic agent based on identification of a peptide biomarker in a biological sample from a subject (described further herein). It can be administered to patients confirmed to have

Biologically active moiety (BM)

In some embodiments of the therapeutic agent (or activatable therapeutic agent, or non-natural activatable therapeutic agent), the biologically active moiety (BM) may comprise a biologically active peptide (BP). Biologically active peptides (BPs) may include antibodies, cytokines, cellular receptors or fragments thereof. A biologically active polypeptide (BP) can include a binding moiety that has binding affinity for a target cell marker on a target tissue or cell. A target cell marker can be an effector cell antigen expressed on the surface of an effector cell. A binding moiety can be an antibody. The antibody may be selected from the group consisting of Fv, Fab, Fab', Fab'-SH, nanobodies (also known as single domain antibodies or V _HH ), linear antibodies and single chain variable fragments (scFv).

In some embodiments of the therapeutic agent (or activatable therapeutic agent, or non-natural activatable therapeutic agent), the binding moiety can be a first binding moiety, the target cell marker can be a first target cell marker, and the biologically active polypeptide ( BP) may further comprise a second binding moiety linked directly or indirectly to the first binding moiety. The second binding moiety can have binding affinity for a second target cell marker on a target tissue or cell. The second target cell marker may be a marker on tumor cells or cancer cells. The second binding moiety may be an antibody. The second binding moiety can be an antibody selected from the group consisting of Fv, Fab, Fab', Fab'-SH, nanobodies (also known as single domain antibodies or V _HH ), linear antibodies and single chain variable fragments (scFv).

In some embodiments as disclosed herein, a biologically active moiety (BM) or biologically active peptide (BP) is specific for a given target (or a given number of targets) when used in vivo or when used in an in vitro assay. binding specificity or/and another desired biological characteristic. For example, a BM or BP can be an agonist, receptor, ligand, antagonist, enzyme, antibody (eg monospecific or bispecific) or hormone. Of particular interest are BMs or BPs used in or known to be useful for a disease or disorder, wherein the native BM or BP has a relatively short elimination half-life and (optionally by cleavage of a spacer sequence from the conjugate or fusion polypeptide) is of interest. Its pharmacokinetic parameters (which can be released) will allow for less frequent dosing or enhanced pharmacological effects. Also of interest is a BM or BP with a relatively narrow therapeutic window between the minimum effective dose or blood concentration (C _min ) and the maximum tolerated dose or blood concentration (C _max ). In such cases, linkage of BMs or BPs in conjugates or fusion polypeptides comprising selected masking moieties such as XTEN can improve these properties, making them more suitable as therapeutic or prophylactic agents compared to BMs or BPs not linked to masking moieties such as XTEN. can make it useful. The BM or BP comprised in the compositions of the present invention as described herein can be used for glucose and insulin disorders, metabolic disorders, cardiovascular disorders, coagulation and bleeding disorders, growth disorders or conditions, endocrine disorders, eye disorders, kidney disorders, liver disorders, tumorigenic conditions , inflammatory conditions, autoimmune conditions, and the like.

In some embodiments of the compositions disclosed herein, when the biologically active moiety is a biologically active peptide (BP), the BP is an amino acid sequence (eg (e.g., more fully described in the Glucose Regulating Peptides section below), or the amino acid sequences of the metabolic disorder and cardiology related proteins set forth in Table 3d (e.g., more fully described in the Metabolic Diseases and Cardiovascular Proteins section below), or the amino acid sequence of a growth hormone set forth in Table 3f (e.g., more fully described in the Growth Hormone Proteins section below), or the amino acid sequence of a cytokine set forth in Table 3g (e.g., more fully described in the Cytokine section below). as fully described), or at least (about) 80% sequence identity (e.g., at least (about) 81 %, at least (about) 82%, at least (about) 83%, at least (about) 84%, at least (about) 85%, at least (about) 86%, at least (about) 87%, at least (about) 88%, at least ( About) 89%, at least (about) 90%, at least (about) 91%, at least (about) 92%, at least (about) 93%, at least (about) 94%, at least (about) 95%, at least (about) ) 96%, at least (about) 97%, at least (about) 98%, at least (about) 99%, or 100% sequence identity. , the sequence of BP may contain one or more substitutions shown in Table 4 (eg, those more fully described below).

In some embodiments of the compositions disclosed herein, where the biologically active moiety is a biologically active peptide (BP), the BP is an antibody (e.g., a monospecific, bispecific, trispecific or multispecific antibody) ( As defined above, the term “antibody” may include, among other things, antibody fragments (eg, as described more fully in the Antibodies section below). An antibody may include a binding domain (or binding moiety) that has binding affinity for an effector cell antigen. The effector cell antigen is an effector selected from plasma cells, T cells, B cells, cytokine induced killer cells (CIK cells), mast cells, dendritic cells, regulatory T cells (RegT cells), helper T cells, myeloid cells and NK cells. It can be expressed on the surface of cells. Effector cell antigens can be expressed on or within effector cells. Effector cell antigens can be expressed on T cells such as CD4+, CD8+ or natural killer (NK) cells. Effector cell antigens can be expressed on the surface of T cells. Effector cell antigens can be expressed on B cells, mast cells, dendritic cells or myeloid cells. The binding domain (or binding moiety) may include VH and VL regions derived from a monoclonal antibody capable of binding human CD3. In some embodiments, where a binding domain (or binding moiety) has binding affinity for CD3, a binding domain (or binding moiety) may have binding affinity for a member of the CD3 complex, which is in a discrete form. or independently all known CD3 subunits of the CD3 complex in combined form; Examples include CD3 epsilon, CD3 delta, CD3 gamma, CD3 zeta, CD3 alpha and CD3 beta. A binding domain (or binding moiety) with binding affinity for CD3 may have binding affinity for CD3 epsilon, CD3 delta, CD3 gamma, CD3 zeta, CD3 alpha or CD3 beta. In some embodiments of the compositions of the present disclosure, the binding domain (or binding moiety) that binds human CD3 can be from an anti-CD3 antibody selected from the group of antibodies set forth in Tables 5a-5e . A binding domain (or binding moiety) that binds human CD3 may comprise VH and VL regions, wherein each VH and VL region is a paired pair of anti-CD3 antibodies selected from those set forth in Table 5a or Table 5d. at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% of the VL and VH sequences %, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99%, or 100% sequence identity. A binding domain (or binding moiety) that binds human CD3 may comprise VH and VL regions, wherein each VH and VL region is at least identical to the paired VL and VH sequences of the huUCHT1 anti-CD3 antibody of Table 5a. (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95%, or at least (about) 95% ) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99%, or 100% sequence identity. A binding domain (or binding moiety) that binds human CD3 may comprise a CDR-H1 region, a CDR-H2 region, a CDR-H3 region, a CDR-L1 region, a CDR-L2 region and a CDR-H3 region, wherein Each region can be derived from a monoclonal antibody selected from the group of antibodies set forth in Tables 5a-5b or Table 5d . Each binding domain (or binding moiety) that binds human CD3 is independently at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least the corresponding FR set forth in Table 5c. (about) 93%, or at least (about) 94%, or at least (about) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 98% ) may include FRs exhibiting 99% or 100% sequence identity. The binding domain (or binding moiety) that binds human CD3 is at least (about) 90%, or at least ( about ) 91%, or at least (about) 92%, or at least ( about) 93%, or at least (about) 94%, or at least (about) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) single chain variable fragment (scFv) sequences exhibiting 99% or 100% sequence identity. In the foregoing embodiments, the VH and/or VL domains may be configured as scFvs, diabodies, single domain antibodies or single domain camelid antibodies. An antibody may include a binding domain (or binding moiety) that has a specific binding affinity for a tumor-specific marker or antigen of a target cell (or target antigen). Tumor specific markers or antigens of target cells are alpha 4 integrin, Ang2, B7-H3, B7-H6 (e.g. its natural ligand Nkp30 which is not an antibody fragment), CEACAM5, cMET, CTLA4, FOLR1, EpCAM (epithelial cell adhesion molecule), CCR5, CD19, HER2, HER2 neu, HER3, HER4, HER1 (EGFR), PD-L1, PSMA, CEA, TROP-2, MUC1 (mucin), MUC-2, MUC3, MUC4, MUC5AC, MUC5B , MUC7, MUC16 βhCG, Lewis-Y, CD20, CD33, CD38, CD30, CD56 (NCAM), CD133, ganglioside GD3, 9-O-acetyl-GD3, GM2, Globo H, Fucosyl GM1, GD2, Carbonic Anhydrase IX, CD44v6, Nectin-4, Sonic Hedgehog (Shh), Wue-1, Plasma Cell Antigen 1 (PC-1), Melanoma Chondroitin Sulfate Proteoglycan (MCSP), CCR8, prostate 6-dural epithelial antigen (STEAP), mesothelin, A33 antigen, prostate stem cell antigen (PSCA), Ly-6, desmoglein 4, fetal acetylcholine receptor (fnAChR), CD25, cancer antigen 19- 9 (CA19-9), cancer antigen 125 (CA-125), Müller inhibitor receptor type II (MISIIR), sialylated Tn antigen (sTN), fibroblast activating antigen (FAP), endosialin (CD248), epidermal Growth factor receptor variant III (EGFRvIII), tumor-associated antigen L6 (TAL6), SAS, CD63, TAG72, Thomsen-Friedenreich antigen (TF-antigen), insulin-like growth factor I receptor (IGF-IR), Cora antigen , CD7, CD22, CD70 (e.g., natural ligand that is not an antibody fragment, CD27), CD79a, CD79b, G250, MT-MMP, fibroblast activation antigen (FAP), alpha-fetoprotein (AFP), VEGFR1, VEGFR2 , DLK1, SP17, ROR1, EphA2, ENPP3, glypican 3 (GPC3) and TPBG/5T4 (trophoblast glycoprotein). Tumor-specific markers or antigens of target cells include alpha 4 integrin, Ang2, CEACAM5, cMET, CTLA4, FOLR1, EpCAM (epithelial cell adhesion molecule), CD19, HER2, HER2 neu, HER3, HER4, HER1 (EGFR), PD- L1, PSMA, CEA, TROP-2, MUC1 (mucin), Lewis-Y, CD20, CD33, CD38, mesothelin, CD70 (eg, its natural ligand, not an antibody fragment, CD27), VEGFR1, VEGFR2, ROR1 , EphA2, ENPP3, Glypican 3 (GPC3) and TPBG/5T4 (trophoblast glycoprotein). The tumor specific marker or antigen of the target cell can be any of those shown in the "Target" column of Table 6 . A binding domain (or binding moiety) having binding affinity for a tumor-specific marker or an antigen of a target cell may include VH and VL regions, each of which has a “VH sequence” in Table 6 and At least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93% of any one of the paired VL and VH sequences shown in the "VL sequence" column, or at least (about) 94%, or at least (about) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99%, or 100% can represent the sequence identity of. Without limiting the scope, additional exemplary tumor antigen target(s) can be selected from the group consisting of: FGFR2, LIV1, TRK, RET, BCMA, CD71, CD166, SSTR2, cKIT, VISTA, GPNMB, DLL3 , CD123, LAMP1, P-cadherin, ephrin-A4, PTK7, NaPi2b, GCC, C4.4a, mucin 17, FLT3, NKG2D ligand, SLAMF7, IL13a2R, CLL-1/CLEC12A, CD66e, IL3Ra, CD5, ULBP1 , B7H4, CSPG4, SDC1, IL1RAP, survivin, CD138, CD74, TIM1, SLITRK6, CD37, CD142, AXL, ETBR, cadherin 6, FGFR3, CA6, CanAg (a novel glycoform of Muc 1) , integrin alpha V, Cripto 1 (TDGF1), CD352 and NOTCH3.

The bioactivity of the BP embodiments described herein can be assessed using assays or measured/determined parameters as described herein and is at least (about) 40%, or at least (about) 50%, compared to the corresponding native BP sequence. %, or at least (about) 55%, or at least (about) 60%, or at least (about) 70%, or at least (about) 80%, or at least (about) 90%, or at least (about) 95% or more Such sequences that retain activity would be considered suitable for inclusion in the compositions of the present disclosure.

glucose regulating peptides

Endocrine and obesity-related diseases or disorders have reached epidemic proportions in most developed countries and represent a significant and increasing health care burden in most developed countries, and involve a variety of conditions affecting the body's organs, tissues and circulatory system. Of particular concern are endocrine and obesity related diseases and disorders. Chief among these is diabetes, which is one of the leading causes of death in the United States. Diabetes is divided into two major subclasses, type 1, also known as juvenile diabetes or insulin-dependent diabetes mellitus (IDDM), and type 2, also known as adult-onset diabetes or non-insulin dependent diabetes mellitus (NIDDM). Type 1 diabetes is a form of autoimmune disease that completely or partially destroys the insulin-producing cells of the pancreas in such subjects and requires the use of exogenous insulin for life. Transient complications can occur even in well-managed subjects, some of which are life-threatening.

In patients with type 2 diabetes, elevated blood glucose levels after a meal do not adequately stimulate the pancreas to produce insulin. Additionally, peripheral tissues are generally resistant to the effects of insulin, and these subjects often have higher than normal plasma insulin levels (hyperinsulinemia) as the body attempts to overcome insulin resistance. In advanced disease states, insulin secretion is also impaired.

Insulin resistance and hyperinsulinemia are also associated with two other metabolic disorders that pose significant health risks: impaired glucose tolerance and metabolic obesity. Impaired glucose tolerance is characterized by normal glucose levels before meals and a tendency for levels to rise after meals (hyperglycemia). These individuals are considered to be at higher risk for diabetes and coronary artery disease. Obesity is also a risk factor for a group of conditions called insulin resistance syndrome or "syndrome X", as are hypertension, coronary artery disease (atherosclerosis) and lactic acidosis and related disease conditions. Although the etiology of obesity is believed to be multifactorial, the fundamental problem is that in obesity, nutrient availability and energy expenditure are not balanced until excess adipose tissue is present. Other related diseases or disorders include, but are not limited to, gestational diabetes, juvenile diabetes, obesity, excessive appetite, insufficient satiety, metabolic disorders, glucagonoma, retinal neurodegenerative processes, and the "honeymoon period" of type 1 diabetes.

Dyslipidemia occurs frequently among diabetic patients and is usually characterized by elevated plasma triglycerides in the blood, low HDL (high-density lipoprotein) cholesterol, normal to elevated levels of LDL (low-density lipoprotein) cholesterol, and increased levels of small, dense lipids. Characterized by LDL particles. Dyslipidemia is a major cause of the increased incidence of coronary events and death among diabetic subjects.

Most metabolic processes in glucose homeostasis and insulin response are regulated by a number of peptides and hormones, and many of these peptides and hormones as well as their analogues have found use in the treatment of metabolic diseases and disorders. Many of these peptides tend to be highly homologous to each other even when they have opposite biological functions. Glucose-increasing peptides are exemplified by the peptide hormone glucagon, and glucose-lowering peptides include exendin-4, glucagon-like peptide 1 and amylin. However, the use of therapeutic peptides and/or hormones has had limited success in the management of these diseases and disorders, even when augmented by the use of small molecule drugs. Dosage optimization is particularly important for drugs and biologics used in the treatment of metabolic diseases with a narrow therapeutic window. In general, peptides involved in hormone and glucose homeostasis often have a narrow therapeutic window. The narrow therapeutic window, coupled with the fact that these hormones and peptides generally have short half-lives, require frequent administration to achieve clinical benefit, making management of these patients difficult. Chemical modifications to therapeutic proteins, such as pegylation, can modify in vivo clearance and subsequent serum half-life, but require additional manufacturing steps and result in a heterogeneous final product. In addition, unacceptable side effects due to chronic administration have been reported. Alternatively, genetic modifications that fuse the Fc domain to a therapeutic protein or peptide increase the size of the therapeutic protein, reducing its clearance through the kidneys and facilitating recycling from lysosomes by the FcRn receptor. Unfortunately, the Fc domain does not fold efficiently during recombinant expression and tends to form insoluble precipitates known as inclusion bodies. These inclusion bodies must be solubilized and the functional protein must be renatured, which is a time consuming, inefficient and costly procedure.

In some embodiments of the compositions of the present disclosure, the biologically active peptides (BPs) may include peptides involved in glucose homeostasis, insulin resistance and obesity (collectively, “glucose modulating peptides”), the compositions comprising glucose, It is useful in the treatment of insulin and obesity disorders, diseases and related conditions. A glucose regulating peptide may include any protein of biological, therapeutic or preventive interest or function useful for preventing, treating, mediating or ameliorating a disease, disorder or condition of glucose homeostasis or insulin resistance or obesity. Suitable glucose regulating peptides that can be linked to a masking moiety (eg XTEN) can include any biologically active polypeptide that increases the glucose dependent secretion of insulin by pancreatic beta cells or potentiates the action of insulin. Glucose regulating peptides may also include any biologically active polypeptide that stimulates proinsulin gene transcription in pancreatic beta cells. Furthermore, glucose regulating peptides may also include any biologically active polypeptide that slows gastric emptying time and reduces food intake. Glucose regulating peptides may also include any biologically active polypeptide that inhibits glucagon release from alpha cells of islets of Langerhans. Table 3a provides a non-limiting list of glucose regulating peptide sequences that can be included in the compositions of the present disclosure. In some embodiments of the compositions disclosed herein, where the biologically active moiety can be a biologically active peptide (BP), the BP has at least (about) 80% sequence identity (e.g., For example, at least (about) 81%, at least (about) 82%, at least (about) 83%, at least (about) 84%, at least (about) 85%, at least (about) 86%, at least (about) 87% %, at least (about) 88%, at least (about) 89%, at least (about) 90%, at least (about) 91%, at least (about) 92%, at least (about) 93%, at least (about) 94% , at least (about) 95%, at least (about) 96%, at least (about) 97%, at least (about) 98%, at least (about) 99%, or 100% sequence identity). can

Table 3a. glucose regulating peptides

"Adrenomedullin" or "ADM" refers to the human adrenomedullin peptide hormone and species and sequence variants thereof that retain at least some of the biological activities of mature ADM. ADM is generated from the 185 amino acid preprohormone through sequential enzymatic cleavage and amidation to yield a 52 amino acid bioactive peptide with an estimated plasma half-life of 22 minutes. The ADM-containing fusion proteins of the present invention may find particular use in diabetics for their stimulatory effect on insulin secretion from islet cells for glucose regulation or in subjects exhibiting persistent hypotension. The complete genomic substructure for human AM has been reported (Ishimitsu, et al., Biochem. Biophys. Res. Commun 203:631-639 (1994)) and analogs of ADM peptides have been cloned as described in US Pat. No. 6,320,022. It became.

"Amylin" means a human peptide hormone, referred to as amylin, pramlintide, and species variants thereof, as described in U.S. Patent No. 5,234,906, which has at least some of the biological activities of mature amylin. Amylin is a 37 amino acid polypeptide hormone released along with insulin by pancreatic beta cells in response to nutrient intake (Koda et al., Lancet 339:1179-1180. 1992), which involves the incorporation of glucose into glycogen. It has been reported to regulate several key pathways of carbohydrate metabolism. The amylin-containing fusion proteins of the present invention may find particular use in diabetics and obesity for regulating gastric emptying, inhibiting glucagon secretion and food intake, and thereby influencing glucose availability in the circulation. Thus, the fusion protein can complement the action of insulin, which regulates the rate of glucose clearance from circulation and glucose uptake by peripheral tissues. Amylin analogs were cloned as described in U.S. Patent Nos. 5,686,411 and 7,271,238. Amylin mimetics can be produced that retain biological activity. For example, pramlintide has the sequence KCNTATCATNRLANFLVHSSNNFGPILPPTNVGSNTY (SEQ ID NO: 271), wherein amino acids from the rat amylin sequence replace amino acids from the human amylin sequence. In one embodiment, the invention contemplates a fusion protein comprising an amylin mimetic of the sequence KCNTATCATX ₁ RLANFLVHSSNNFGX ₂ ILX ₂ X ₂ TNVGSNTY (SEQ ID NO: 275), wherein X ₁ is independently N or Q and X ₂ is independently S, P or G. In one embodiment, an amylin mimetic incorporated into a composition of the present disclosure may have the sequence KCNTATCATNRLANFLVHSSNNFGGILGGTNVGSNTY (SEQ ID NO: 276). In another embodiment where an amylin mimetic is used at the C-terminus of the composition, the mimetibody can have the sequence KCNTATCATNRLANFLVHSSNNFGGILGGTNVGSNTY(NH ₂ ) (SEQ ID NO: 276).

"Calcitonin" (CT) refers to the human calcitonin protein and its species and sequence variants, including salmon calcitonin ("sCT"), which has some of the biological activity of mature CT. CT is a 32 amino acid peptide cleaved from a large prohormone of the thyroid gland that appears to function in the nervous and vascular systems, but has also been reported as a potent hormonal mediator of the satiety reflex. CT is named for its secretion and its rapid hypocalcemic effect in response to induced hypercalcemia. It is produced and secreted from neuroendocrine glands in the thyroid gland called C cells. CT has an effect on osteoclasts, and inhibition of osteoclast function by CT reduces bone resorption. The in vitro effects of CT include rapid loss of wrinkled borders and reduced release of lysosomal enzymes. The primary function of CT(1-32) is to fight acute hypercalcemia in emergency situations and/or to protect the skeleton during periods of “calcium stress” such as growth, pregnancy and lactation. (Reviewed in Becker, JCEM, 89(4): 1512-1525 (2004) and Sexton, Current Medicinal Chemistry 6: 1067-1093 (1999)). The calcitonin-containing fusion proteins of the present invention may find particular use for the treatment of osteoporosis and as a treatment for Paget's disease of the bone. Synthetic calcitonin peptides were prepared as described in US Pat. Nos. 5,175,146 and 5,364,840.

“Cacitonin gene related peptide” or “CGRP” refers to species and sequence variants thereof that have at least some of the biological activity of human CGRP peptides and mature CGRP. Calcitonin gene-related peptides are members of the calcitonin family of peptides, which exist in humans in two forms, α-CGRP (37 amino acid peptide) and β-CGRP. CGRP has 43-46% sequence identity with human amylin. The CGRP-containing fusion proteins of the present invention may find particular use in reducing diabetes-related prevalence, ameliorating hyperglycemia and insulin deficiency, inhibiting lymphocyte infiltration into islets, and protecting beta cells against autoimmune destruction. Methods for preparing synthetic and recombinant CGRP are described in US Pat. No. 5,374,618.

“Cholecystokinin” or “CCK” refers to human CCK peptides and species and sequence variants thereof that have at least some of the biological activities of mature CCK. CCK-58 is the mature sequence, and the CCK-33 amino acid sequence, first identified in humans, is the major circulating form of the peptide. The CCK family also includes an eight amino acid C-terminal fragment ("CCK-8") in vivo, pentagastrin or CCK-5, the C-terminal peptide CCK (29-33), and the C-terminal tetrapeptide CCK (30-33 ), including CCK-4. CCK is a peptide hormone of the gastrointestinal system responsible for stimulating the digestion of fats and proteins. The CCK-33 and CCK-8 containing fusion proteins of the present invention may find particular use in reducing the increase in circulating glucose after meals and enhancing the increase in circulating insulin. Analogs of CCK-8 were prepared as described in US Pat. No. 5,631,230.

“Exendin-3” refers to a glucose regulating peptide isolated from Heloderma horridum and sequence variants thereof that retain some of the biological activity of mature Exendin-3. Exendin-3 amide is a specific exendin receptor antagonist from mediating pancreatic cAMP increase and release of insulin and amylase. Exendin-3 containing fusion proteins of the present invention may find particular use in the treatment of diabetes and insulin resistance disorders. The sequence and methods for its analysis are described in US Pat. No. 5,424,286.

"Exendin-4" refers to a glucose regulating peptide found in the saliva of the venomous large lizard Heloderma suspectum and its species and sequence variants, with the natural 39 amino acid sequence His-Gly-Glu- Gly-Thr-Phe-Thr-Ser-Asp-Leu-Ser-Lys-Gln-Met-Glu-Glu-Glu-Ala-Val-Arg-Leu-Phe-Ile-Glu-Trp-Leu-Lys-Asn- Gly-Gly-Pro-Ser-Ser-Gly-Ala-Pro-Pro-Pro-Ser and homologous sequences, and peptidomimetics and variants thereof; A native sequence obtained from a primate, and a non-natural sequence having at least some of the biological activity of mature exendin-4. Exendin-4 is an incretin polypeptide hormone that reduces blood sugar, stimulates insulin secretion, delays gastric emptying, and improves satiety, providing marked improvement in postprandial hyperglycemia. Exendins have some sequence similarity to members of the glucagon-like peptide family and have the highest identity with GLP-1 (Goke, et al., J. Biol. Chem., 268:19650-55 (1993)). A variety of homologous sequences may be functionally equivalent to native exendin-4 and GLP-1. Conservation of GLP-1 sequences from different species is reviewed by Regulatory Peptides 2001 98 p. 1-12]. Table 3b shows sequences from various species and Table 3c lists synthetic GLP-1 analogues; All of these are contemplated for use in the compositions described herein. Exendin-4 binds at the GLP-1 receptor of insulin-releasing βTC1 cells, and also stimulates somatostatin release and inhibits gastrin release in the isolated stomach (Goke, et al., J. Biol. Chem . 268:19650-55). , 1993). As a mimetic of GLP-1, exendin-4 exhibits similar broad biological activity, but has a longer half-life than GLP-1, with an average elimination half-life of 2.4 hours. Exenatide is a synthetic version of exendin-4 marketed as Byetta. However, due to its short half-life, exenatide is currently administered twice daily, limiting its use. Exendin-4 containing fusion proteins of the present invention may find particular use in the treatment of diabetes and insulin resistance disorders.

'Fibroblast growth factor 21', or "FGF-21", refers to the human protein encoded by the FGF21 gene, or species and sequence variants thereof that have at least some of the biological activities of mature FGF21. FGF-21 stimulates glucose uptake in adipocytes, but not in other cell types. This effect is additive to the activity of insulin. Injection of FGF21 in ob/ob mice results in an increase in Glut1 in adipose tissue. FGF21 also protects animals from diet-induced obesity when overexpressed in transgenic mice and lowers blood glucose and triglyceride levels when administered to diabetic rodents (Kharitonenkov A, et al., (2005). “FGF- 21 as a novel metabolic regulator” (J. Clin. Invest. 115: 1627-35). The FGF-21 containing fusion proteins of the present invention may find particular use in the treatment of diabetes, including those resulting in increased energy expenditure, fat utilization and lipid excretion. FGF-21 was cloned as disclosed in US Pat. No. 6,716,626.

"FGF-19", or "fibroblast growth factor 19", refers to the human protein encoded by the FGF19 gene, or species and sequence variants thereof that have at least some of the biological activities of mature FGF-19. FGF-19 is a protein member of the fibroblast growth factor (FGF) family. FGF family members possess a wide range of mitogenic and cell survival activities and are involved in a variety of biological processes. FGF-19 increases hepatic expression of the leptin receptor, metabolic rate, stimulates glucose uptake in adipocytes, and results in weight loss in an obese mouse model (Fu, L, et al. FGF-19-containing fusion of the present invention). The protein increases metabolic rate and may find particular use in diet and reversal of leptin-deficient diabetes FGF-19 was cloned and expressed as described in US Patent Application No. 20020042367.

"Gastrin" refers to human gastrin peptides, truncated versions, and species and sequence variants thereof that have at least some of the biological activity of mature gastrin. Gastrin is a linear peptide hormone produced by the G cells of the duodenum and in the pyloric sinus of the stomach and released into the bloodstream. Gastrin is found primarily in three forms: gastrin-34 ("large gastrin"); gastrin-17 ("little gastrin"); Gastrin-14 ("minigastrin"). It shares sequence homology with CCK. The gastrin-containing fusion proteins of the present invention may find particular use in the treatment of obesity and diabetes for glucose control. Gastrin was synthesized as described in US Pat. No. 5,843,446.

"Ghrelin" refers to the human hormone that induces satiety, or species and sequence variants thereof, including natural, processed 27 or 28 amino acid sequences and homologous sequences. Ghrelin is mainly produced by the epsilon cells of the pancreas, which stimulate hunger, and the P/D1 cells lining the human stomach, and is considered the hormone that corresponds to leptin. Ghrelin levels increase before meals and decrease after meals, increasing food intake and possibly leading to increased fat mass by actions exerted at the level of the hypothalamus. Ghrelin also stimulates the release of growth hormone. Ghrelin is acylated at serine residues by n-octanoic acid; This acylation is essential for binding to the GHS1a receptor and the ability of ghrelin to release GH. The ghrelin-containing fusion proteins of the present invention may find particular use as agonists, for example in gastrointestinal motility disorders, selectively stimulating motility of the gastrointestinal tract, accelerating gastric emptying, or stimulating the release of growth hormone. As described in U.S. Patent No. 7,385,026, ghrelin analogs with sequence substitutions or truncated variants find particular use as fusion partners to XTEN for use as antagonists for improved glucose homeostasis, treatment of insulin resistance, and treatment of obesity. can do. Isolation and characterization of ghrelin has been reported (Kojima M, et al. , Ghrelin is a growth-hormone-releasing acylated peptide from stomach. Nature. 1999;402(6762):656-660.) and a synthetic analog has been reported in U.S. Patent No. 6,967,237. prepared by peptide synthesis as described in .

"Glucagon" refers to human glucagon glucose regulating peptide, or species and sequence variants thereof, including the natural 29 amino acid sequence and homologous sequences; Natural and non-natural sequence variants from primates that have at least some of the biological activity of mature glucagon. As used herein, the term “glucagon” also includes peptidomimetics of glucagon. Natural glucagon is produced in the pancreas and released when blood sugar levels start to drop too low, allowing the liver to convert stored glycogen into glucose, which is then released into the bloodstream. Although the action of glucagon is opposite to that of insulin, which signals the body's cells to take up glucose from the blood, glucagon also stimulates the release of insulin, which makes the newly available glucose in the bloodstream available for uptake and use by insulin-dependent tissues. can The glucagon-containing fusion proteins of the present invention may find particular use in maintaining glucose homeostasis in diabetes and increasing blood glucose levels in individuals with residual hepatic glycogen stores. Glucagon was cloned as disclosed in US Pat. No. 4,826,763.

“GLP-1” means human glucagon-like peptide-1 and sequence variants thereof that retain at least some of the biological activities of mature GLP-1. The term “GLP-1” includes human GLP-1(1-37), GLP-1(7-37), GLP-1(7-36)amide. GLP-1 stimulates insulin secretion, but only during periods of hyperglycemia. The safety of GLP-1 compared to insulin is enhanced by this property and the observation that the amount of insulin secreted is proportional to the magnitude of hyperglycemia. The biological half-life of GLP-1(7-37)OH is only 3 to 5 minutes (US Pat. No. 5,118,666). The GLP-1 containing fusion proteins of the present invention may find particular use in the treatment of diabetes and insulin resistance disorders for glucose control. GLP-1 was cloned and derivatives prepared as described in US Pat. No. 5,118,666. Non-limiting examples of glucagon-like peptide sequences from various species and their synthetic analogues are shown in Tables 3b-3c . In some embodiments of the compositions disclosed herein, where the biologically active moiety can be a biologically active peptide (BP), the BP is at least (about ) 80% sequence identity (e.g., at least (about) 81%, at least (about) 82%, at least (about) 83%, at least (about) 84%, at least (about) 85%, at least (about) 86%, at least (about) 87%, at least (about) 88%, at least (about) 89%, at least (about) 90%, at least (about) 91%, at least (about) 92%, at least (about) 93% %, at least (about) 94%, at least (about) 95%, at least (about) 96%, at least (about) 97%, at least (about) 98%, at least (about) 99%, or 100% sequence identity ).

Table 3b. Representative naturally occurring GLP-1 homologues as BP candidates

Table 3c. Representative GLP-1 synthetic analogs

The GLP natural sequence can be described by several sequence motifs presented below. Letters in parentheses indicate allowed amino acids at each sequence position: [HVY] [AGISTV] [DEHQ] [AG] [ILMPSTV] [FLY] [DINST] [ADEKNST] [ADENSTV] [LMVY] [ANRSTY] [EHIKNQRST] [AHILMQVY] [LMRT] [ADEGKQS] [ADEGKNQSY] [AEIKLMQR] [AKQRSVY] [AILMQSTV] [GKQR] [DEKLQR] [FHLVWY] [ILV] [ADEGHIKNQRST] [ADEGNRSTW] [GILVW] [AIKLMQSV] [ADGIKNQRST] [GKRSY ]. In addition, synthetic analogs of GLP-1 may be useful as fusion partners for masking moieties (eg, XTEN) to create fusion compositions with biological activity useful for the treatment of glucose-related disorders. Additional sequences homologous to exendin-4 or GLP-1 can be found by standard homology search techniques.

"GLP-2" means human glucagon-like peptide-2 and sequence variants thereof that retain at least some of the biological activities of mature GLP-2. More specifically, GLP-2 is a peptide of 33 amino acids co-secreted with GLP-1 from enteroendocrine cells of the small and large intestine.

“IGF-1” or “insulin-like growth factor 1” refers to human IGF-1 protein and species and sequence variants thereof that have at least some of the biological activities of mature IGF-1. IGF-1, once called somatomedin C, is a polypeptide protein anabolic hormone similar in molecular structure to insulin, which regulates the action of growth hormone. IGF-1 consists of 70 amino acids and is mainly produced as an endocrine hormone in the liver and also in target tissues in a paracrine/autocrine manner. The IGF-1 containing fusion proteins of the present invention may find particular use in the treatment of diabetes and insulin resistance disorders for glucose control. IGF-1 was cloned and expressed in E. coli and yeast as described in US Pat. No. 5,324,639.

“IGF-2” or “insulin-like growth factor 2” refers to human IGF-2 protein and species and sequence variants thereof that have at least some of the biological activities of mature IGF-2. IGF-2, a polypeptide protein hormone similar in molecular structure to insulin, plays a major role as a growth-stimulating hormone during pregnancy. IGF-2 is described by Bell GI, et al. Isolation of the human insulin-like growth factor genes: insulin-like growth factor II and insulin genes are contiguous. Proc Natl Acad Sci US A. 1985. 82(19):6450-4.

“INGAP” or “isletogenesis-associated protein” or “pancreatic beta cell growth factor” refers to a human INGAP peptide and species and sequence variants thereof that have at least some of the biological activities of mature INGAP. INGAP can initiate ductal cell proliferation, which is a prerequisite for islet neogenesis. The INGAP-containing fusion proteins of the present invention may find particular use in the treatment or prevention of diabetes and insulin resistance disorders. INGAP is described in R Rafaeloff R, et al ., Cloning and sequencing of the pancreatic islet neogenesis associated protein (INGAP) gene and its expression in islet neogenesis in hamsters. J Clin Invest. 1997. 99(9): 2100-2109.

“Intermedin” or “AFP-6” refers to human intermedin peptides and species and sequence variants thereof that retain at least some of the biological activities of mature intermedins. Intermedins are ligands for calcitonin receptor-like receptors. Intermedin treatment not only reduces blood pressure in normal and hypertensive subjects, but also inhibits gastric emptying activity and is related to glucose homeostasis. The intermedin-containing fusion proteins of the present invention may find particular use in the treatment of diabetes, insulin resistance disorders and obesity. Intermedin peptides and variants were cloned as described in US Pat. No. 6,965,013.

"Leptin" refers to the biologically active D-isoform, or fragments and sequence variants thereof, as well as naturally occurring leptin from any species. Leptin plays an important role in regulating energy intake and energy expenditure, including appetite and metabolism. The leptin-containing fusion proteins of the present invention may find particular use in the treatment of diabetes, insulin resistance disorders and obesity for glucose control. Leptin is the polypeptide product of the ob gene as described in International Patent Publication No. WO 96/05309. Leptin was cloned as described in U.S. Pat. No. 7,112,659, and leptin analogs and fragments were cloned as described in U.S. Pat. Nos. 5,521,283, U.S. Pat. No. 5,532,336, PCT/US96/22308 and PCT/US96/01471.

“Neuromedin” refers to peptides of the neuromedin family, including neuromedin U and S peptides, and sequence variants thereof. The naturally active human Neuromedin U peptide hormone is Neuromedin-U25, particularly its amide form. Of particular interest are their processed active peptide hormones and analogs, derivatives and fragments thereof. The Neuromedin U family includes various truncated or splice variants, such as FLFHYSKTQKLGKSNVVEELQSPFASQSRGYFLFRRPRN (SEQ ID NO: 409). An example of the neuromedin S family is human neuromedin S with the sequence ILQRGSGTAAVDFTKKDHTATWGRPFFLFRPRN (SEQ ID NO: 267), especially its amide form. Neuromedin fusion proteins of the present invention may find particular use in the treatment of obesity, diabetes, reduced food intake and other related conditions and disorders described herein. Of particular interest are neuromedin modules in combination with amylin family peptides, exendin peptide family or GLP I peptide family modules.

“Oxintomodulin” or “OXM” refers to human oxyntomodulin and species and sequence variants thereof that retain at least some of the biological activities of mature OXM. OXM is a 37 amino acid peptide produced in the colon that contains the 29 amino acid sequence of glucagon followed by an 8 amino acid carboxyterminal extension. OXM has been found to suppress appetite. The OXM-containing fusion proteins of the present invention may find particular use in the treatment of diabetes, insulin resistance disorders, obesity for glucose control, and may be used in weight loss therapy.

“PYY” refers to human peptide YY polypeptides and species and sequence variants thereof that have at least some of the biological activities of mature PYY. PYY includes both PYY _1-36 and PYY _3-36 with a human full-length, 36 amino acid peptide, PP folding structural motif. PYY inhibits gastric motility and increases water and electrolyte absorption in the colon. PYY can also inhibit pancreatic secretion. The PPY-containing fusion proteins of the present invention may find particular use in the treatment of diabetes, insulin resistance disorders and obesity for glucose control. Analogs of PYY were prepared as described in US Pat. Nos. 5,604,203, 5,574,010 and 7,166,575.

"Urocortin" means the human urocortin peptide hormone and sequence variants thereof that retain at least some of the biological activities of mature urocortin. There are three human urocortins Ucn-1, Ucn-2 and Ucn-3. Additional urocortin and analogs are described in US Pat. No. 6,214,797. Eurocortins Ucn-2 and Ucn-3 have food intake inhibitory, antihypertensive, cardioprotective and contractile promoting properties. Ucn-2 and Ucn-3 have the ability to inhibit chronic HPA activation following stressful stimuli such as diet/fasting and do not activate CRF-R1, which is specific for the CRF type 2 receptor and mediates ACTH release. Therapeutics comprising urocortin, eg Ucn-2 or Ucn-3, may be useful for vasodilation and thus cardiovascular applications such as chronic heart failure. The urocortin-containing fusion proteins of the present invention also stimulate ACTH release, hypertension due to vasodilatory effects, inflammation mediated through other than ACTH elevation, hyperthermia, appetite disorders, congestive heart failure, stress, anxiety and conditions associated with psoriasis. It may find particular use in treatment or prevention. Urocortin-containing fusion proteins can also be combined with natriuretic peptide modules, amylin family and exendin family or GLP1 family modules to provide enhanced cardiovascular benefits. For example, it can treat CHF by providing a beneficial vasodilator effect.

Metabolic disease and cardiovascular proteins

Metabolic and cardiovascular diseases represent a significant health care burden in most developed countries and cardiovascular disease remains the leading cause of death and disability in the United States and most European countries. Metabolic diseases and disorders include a wide variety of conditions that affect the organs, tissues and circulatory system of the body. Foremost among these is diabetes, which is one of the leading causes of death in the United States as it results in pathology and metabolic dysfunction in both the vasculature, central nervous system, major organs and peripheral tissues. Insulin resistance and hyperinsulinemia are also associated with two other metabolic disorders that pose significant health risks: impaired glucose tolerance and metabolic obesity. Impaired glucose tolerance is characterized by normal glucose levels before meals and a tendency for levels to rise after meals (hyperglycemia). These individuals are considered to be at higher risk for diabetes and coronary artery disease. Obesity is also a risk factor for a group of conditions called insulin resistance syndrome or "Syndrome X", as are hypertension, coronary artery disease (atherosclerosis) and lactic acidosis and related disease conditions. Although the etiology of obesity is believed to be multifactorial, the fundamental problem is that in obesity, nutrient availability and energy expenditure are not balanced until excess adipose tissue is present.

Dyslipidemia occurs frequently among diabetic patients and subjects with cardiovascular disease, and is generally characterized by elevated plasma triglycerides, low HDL (high-density lipoprotein) cholesterol, normal to elevated levels of LDL (low-density lipoprotein) cholesterol, and elevated plasma triglycerides in the blood. It is characterized by parameters such as the level of small and dense LDL particles. Dyslipidemia and hypertension are major causes of increased incidence of coronary events, renal disease and death in subjects with metabolic diseases such as diabetes and cardiovascular disease.

Cardiovascular diseases include, among others, aneurysms, angina pectoris, atherosclerosis, cerebrovascular accident (stroke), cerebrovascular disease, congestive heart failure, coronary artery disease, myocardial infarction, reduced cardiac output and peripheral vascular disease, hypertension, hypotension, blood markers (e.g. For example, C-reactive protein, BNP, and enzymes such as CPK, LDH, SGPT, and SGOT), a number of disorders related to the heart, vasculature, and organ systems of the body, symptoms, and changes in clinical parameters may be manifested. .

Most metabolic processes and many cardiovascular parameters are regulated by a number of peptides and hormones ("metabolic proteins"), and many of these peptides and hormones, as well as their analogues, have found use in the treatment of these diseases and disorders. However, the use of therapeutic peptides and/or hormones has had limited success in the management of these diseases and disorders, even when augmented by the use of small molecule drugs. Dosage optimization is particularly important for drugs and biologics used in the treatment of metabolic diseases with a narrow therapeutic window. In general, peptides involved in hormone and glucose homeostasis often have a narrow therapeutic window. The narrow therapeutic window, coupled with the fact that these hormones and peptides generally have short half-lives, require frequent administration to achieve clinical benefit, making management of these patients difficult. Thus, there is still a need for therapeutic agents with a wider therapeutic window and increased efficacy and safety in the treatment of metabolic diseases.

In some embodiments of the composition, a biologically active peptide (BP) as disclosed herein may include a biologically active metabolic protein, and the composition may be useful in the treatment of metabolic and cardiovascular diseases and disorders. A metabolic protein may include any protein of biological, therapeutic or prophylactic interest or function useful in preventing, treating, mediating or ameliorating a metabolic or cardiovascular disease, disorder or condition. Table 3d provides a non-limiting list of such sequences of metabolic BPs that can be included in the compositions (eg, therapeutics) of the present invention. In some embodiments of the compositions disclosed herein, where the biologically active moiety is a biologically active peptide (BP), the BP has at least (about) 80% sequence identity (e.g., At least (about) 81%, at least (about) 82%, at least (about) 83%, at least (about) 84%, at least (about) 85%, at least (about) 86%, at least (about) 87%, at least (about) 88%, at least (about) 89%, at least (about) 90%, at least (about) 91%, at least (about) 92%, at least (about) 93%, at least (about) 94%, at least ( about) 95%, at least (about) 96%, at least (about) 97%, at least (about) 98%, at least (about) 99%, or 100% sequence identity).

Table 3d. Metabolic Disorders and Cardiology Relevant Biologically Active Proteins

“Anti-CD3” refers to the T cell surface protein CD3, including OKT3 (also called muromonab) and humanized anti-CD3 monoclonal antibodies (KC Herold et al., New England Journal of Medicine 346:1692-1698. 2002). monoclonal antibodies to, species and sequence variants thereof. Anti-CD3 binds to the T cell receptor complex present on all differentiated T cells and prevents T cell activation and proliferation. The anti-CD3 containing fusion proteins of the present invention can be used to treat newly developed type 1 diabetes, including using anti-CD3 as a therapeutic effector as well as a targeting moiety for a second therapeutic BP in a composition of the present disclosure. You can find a special use for slowing down. Sequences for the variable regions and generation of anti-CD3 are described in US Pat. Nos. 5,885,573 and 6,491,916.

“IL-1ra” refers to the human IL-1 receptor antagonist protein and its species and sequence variants, including anakinra (Kineret®), a sequence variant that has at least some of the biological activity of mature IL-1ra. Human IL-1ra is a mature glycoprotein composed of 152 amino acid residues. The inhibitory action of IL-1ra occurs due to binding to the type I IL-1 receptor. This protein has an intrinsic molecular weight of 25 kDa, and this molecule shows limited sequence homology to IL-1α (19%) and IL-1ß (26%). Anakinra is an unglycosylated, recombinant human IL-1ra and differs from endogenous human IL-1ra by the addition of an N-terminal methionine. A commercialized version of anakinra is marketed as Kineret®. It binds to the IL-1 receptor with the same avidity as native IL-1ra and IL-1b, but there is only one receptor-binding motif on IL-1ra compared to these two motifs on IL-1α and IL-1ß. It does not cause receptor activation (signal transduction), which is the effect that occurs by doing so. Anakinra is reported to have 153 amino acids, a size of 17.3 kD, and a half-life of approximately 4-6 hours.

various viral, bacterial, fungal and parasitic infections; intravascular coagulation; high-dose IL-2 therapy; solid tumor; leukemia; Alzheimer's disease; HIV-1 infection; autoimmune disorders; trauma (surgery); hemodialysis; ischemic disease (myocardial infarction); noninfectious hepatitis; asthma; UV irradiation; closed head injury; pancreatitis; peritonitis; graft versus host disease; patients with transplant rejection; and an increase in IL-1 production in healthy subjects after excessive exercise. It has been associated with increased IL-1b production in Alzheimer's disease patients, and there is a possible role for IL1 in the release of amyloid precursor protein. IL-1 is also found in type 2 diabetes, obesity, hyperglycemia, hyperinsulinemia, type 1 diabetes, insulin resistance, retinal neurodegenerative processes, disease states and conditions characterized by insulin resistance, acute myocardial infarction (AMI), acute Coronary artery syndrome (ACS), atherosclerosis, chronic inflammatory disorders, rheumatoid arthritis, degenerative intervertebral disc disease, sarcoidosis, Crohn's disease, ulcerative colitis, gestational diabetes, excessive appetite, insufficient satiety, metabolic disorders, glucagonoma, airway Secretory disorders, osteoporosis, central nervous system disease, restenosis, neurodegenerative diseases, renal failure, congestive heart failure, renal syndrome, liver cirrhosis, pulmonary edema, hypertension, disorders in which reduced food intake is desirable, irritable bowel syndrome, myocardial infarction, stroke, surgery Post-catabolic changes, hibernating heart muscle, diabetic cardiomyopathy, insufficient urinary sodium excretion, excessive urinary potassium concentration, toxic hypervolemia-related conditions or disorders, polycystic ovary syndrome, dyspnoea, chronic skin ulcers, nephropathy, left ventricular systolic function Disorders, Gastrointestinal Diarrhea, Postoperative Dumping Syndrome, Irritable Bowel Syndrome, Majority Disease Polyneuropathy (CIPN), Systemic Inflammatory Response Syndrome (SIRS), Dyslipidemia, Post-Ischemic Reperfusion Injury and Coronary Heart Disease Risk Factor (CHDRF) associated with diseases such as syndrome. The IL-1ra containing fusion proteins of the present invention may find particular use in the treatment of any of the diseases and disorders described above. IL-1ra was cloned as described in US Pat. Nos. 5,075,222 and 6,858,409.

"Natriuretic peptide" includes atrial natriuretic peptide (ANP), brain natriuretic peptide (BNP or type B natriuretic peptide) and type C natriuretic peptide (CNP); Both human and non-human species and sequence variants thereof that have at least a portion of the biological activity of the mature corresponding natriuretic peptide. Alpha atrial natriuretic peptide (aANP) or (ANP) and brain natriuretic peptide (BNP) and type C natriuretic peptide (CNP) are homologous polypeptide hormones involved in the regulation of body fluid and electrolyte homeostasis. The sequence of a useful form of natriuretic peptide is disclosed in US Patent Publication 20010027181. Examples of ANPs include ANPs from various species, including human ANP (Kangawa et al., BBRC 118:131 (1984)) or swine and rat ANP (Kangawa et al., BBRC 121:585 (1984)). . As a result of sequencing, prepro BNP consists of 134 residues and is cleaved into 108 amino acids Pro BNP. Cleavage of the 32 amino acid sequence from the C-terminal end of proBNP yields the circulating, physiologically active form of human BNP (77-108). Human BNP of 32 amino acids involves the formation of disulfide bonds (Sudoh et al., BBRC 159:1420 (1989)) and US Pat. Nos. 5,114,923, 5,674,710, 5,674,710 and 5,948,761. Compositions containing one or more natriuretic functions may be used for treating hypertension, inducing diuresis, inducing natriuresis, dilating or relaxing blood vessels, binding natriuretic peptide receptors (e.g., NPR-A), μapida from the kidney inhibition of secretion, inhibition of aldosterone secretion from the adrenal gland, treatment of cardiovascular diseases and disorders, reduction, interruption or reversal of cardiac remodeling after a cardiac event or as a result of congestive heart failure, treatment of renal diseases and disorders; It may be useful in the treatment or prevention of ischemic stroke and in the treatment of asthma.

“FGF-2” or heparin binding growth factor 2 refers to human FGF-2 protein and species and sequence variants thereof that retain at least some of the biological activities of their mature counterparts. FGF-2 has been shown to stimulate the proliferation of neural stem cells differentiated into striatal-like neurons and protect striatal neurons in a model of toxin-induced Huntington's disease, and may also be useful in the treatment of cardiac reperfusion injury, endothelial cell growth, anti-aging It can exhibit angiogenic and tumor suppressive properties, promote wound healing and fracture healing of bone. FGF-2 is described by Burgess, W. H. and Maciag, T., Ann. Rev. Biochem., 58:575-606 (1989); See Coulier, F., et al., 1994, Prog. Growth Factor Res. 5:1] and PCT publication WO 87/01728.

"TNF receptor" means the human receptor for TNF and species and sequence variants thereof that have at least some of the biological receptor activity of mature TNFR. The p75 TNF receptor molecule is an extracellular domain of the p75 TNF receptor that is derived from a family of structurally homologous receptors that includes the p55 TNF receptor. TNFα and TNFβ (TNF ligands) compete for binding to the p55 and p75 TNF receptors. The x-ray crystal structure of the complex formed by the extracellular domain of the human p55 TNF receptor and TNFβ was determined (Banner et al. Cell 73:431, 1993 (incorporated herein by reference)).

growth hormone protein

“Growth hormone” or “GH” refers to human growth hormone protein and species and sequence variants thereof, including but not limited to the 191 single chain amino acid human sequence of GH. Thus, GH can be a natural full-length protein, or it can be a truncated fragment or sequence variant that retains at least a portion of the biological activity of the native protein. The effects of GH on body tissues can generally be described as anabolic. Like most other protein hormones, GH works by interacting with specific plasma membrane receptors called growth hormone receptors. There are two known types of human GH (hereafter “hGH”) derived from the pituitary gland: one with a molecular weight of about 22,000 Daltons (22 kD hGH), and one with a molecular weight of about 20,000 Daltons (20 kD hGH) . 20 kD HGH has an amino acid sequence corresponding to that of 22 kD hGH consisting of 191 amino acids except that 15 amino acid residues from 32nd to 46th of 22 kD hGH are missing. Some reports have shown that 20 kD hGH has lower risk and higher activity than 22 kD hGH. The present invention also contemplates the use of 20 kD hGH suitable for use as the biologically active polypeptide for the compositions of the present disclosure.

The present invention relates to any GH homologous sequence, fragment of native sequence, such as a primate, mammal (including livestock), and biological activity or biological function of GH, and/or preventing a GH-related disease, deficiency, disorder or condition; It is contemplated to include in a composition a non-naturally occurring sequence variant useful for treatment, mediation, or amelioration. Non-mammalian GH sequences are well described in the literature. For example, a sequence alignment of fish GH can be found in Genetics and Molecular Biology 2003 26 p.295-300. An evolutionary analysis of algal GH sequences is presented in the Journal of Evolutionary Biology 2006 19 p.844-854. In addition, native sequences homologous to human GH can be found by standard homology search techniques such as NCBI BLAST.

In one embodiment, the GH incorporated into a subject composition may be a recombinant polypeptide having a sequence corresponding to a protein found in nature. In another embodiment, the GH may be a sequence variant, fragment, homologue or mimetic of the native sequence that retains at least a portion of the biological activity of the native GH. Table 3f provides a non-limiting list of GH sequences from various mammalian species included in the compositions of the present disclosure. Any of these GH sequences or homologous derivatives constructed by mixing individual mutations between species or families may be useful in the fusion proteins of the present invention. In some embodiments of the compositions disclosed herein, where the biologically active moiety can be a biologically active peptide (BP), the BP has at least (about) 80% sequence identity (e.g., For example, at least (about) 81%, at least (about) 82%, at least (about) 83%, at least (about) 84%, at least (about) 85%, at least (about) 86%, at least (about) 87% , at least (about) 88%, at least (about) 89%, at least (about) 90%, at least (about) 91%, at least (about) 92%, at least (about) 93%, at least (about) 94%, at least (about) 95%, at least (about) 96%, at least (about) 97%, at least (about) 98%, at least (about) 99%, or 100% sequence identity). there is.

Table 3f. Growth Hormone Amino Acid Sequences from Animal Species

cytokines

BP may be a cytokine. The cytokines included in the composition of the present invention are useful in cancer, rheumatoid arthritis, multiple sclerosis, myasthenia gravis, systemic lupus erythematosus, Alzheimer's disease, schizophrenia, viral infections (eg chronic hepatitis C, AIDS), allergic asthma , retinal neurodegenerative processes, metabolic disorders, insulin resistance and diabetic cardiomyopathy. Cytokines can be particularly useful for treating inflammatory and autoimmune conditions.

BP can be one or more cytokines. Cytokines refer to proteins released by cells (eg, chemokines, interferons, lymphokines, interleukins, and tumor necrosis factors) that can affect cell behavior. Cytokines can be produced by a wide variety of cells, including endothelial cells, fibroblasts and various stromal cells, as well as immune cells such as macrophages, B lymphocytes, T lymphocytes and mast cells. A given cytokine can be produced in more than one cell type. Cytokines may be involved in producing systemic or local immunomodulatory effects.

Certain cytokines can act as pro-inflammatory cytokines. Proinflammatory cytokines refer to cytokines involved in inducing or amplifying an inflammatory response. Pro-inflammatory cytokines can act together with various cells of the immune system, such as neutrophils and leukocytes, to generate an immune response. Certain cytokines can act as anti-inflammatory cytokines. Anti-inflammatory cytokines refer to cytokines involved in the reduction of the inflammatory response. Anti-inflammatory cytokines can in some cases modulate pro-inflammatory cytokine responses. Some cytokines can act as proinflammatory and antiinflammatory cytokines.

Examples of cytokines modulatory by the systems and compositions of the present disclosure include, but are not limited to, lymphokines, monokines, and traditional polypeptide hormones other than human growth hormone. Among cytokines, parathyroid hormone; thyroxine; insulin; proinsulin; relaxin; prorelaxin; glycoprotein hormones such as follicle stimulating hormone (FSH), thyroid stimulating hormone (TSH) and luteinizing hormone (LH); liver growth factor; fibroblast growth factor; prolactin; placental lactogen; tumor necrosis factor-alpha; Müller inhibitor; mouse gonadotropin-associated peptide; inhibin; activin; vascular epithelial growth factor; integrins; thrombopoietin (TPO); nerve growth factors such as NGF-alpha; platelet growth factor; transforming growth factors (TGF) such as TGF-alpha, TGF-beta, TGF-beta1, TGF-beta2, TGF-beta3; insulin-like growth factors-I and -II; erythropoietin (EPO); Flt-3L; stem cell factor (SCF); osteoinductive factor; interferons (IFN) such as IFN-α, IFN-β, IFN-γ; colony stimulating factors (CSFs) such as macrophage-CSF (M-CSF); granulocyte-macrophage-CSF (GM-CSF); granulocyte-CSF (G-CSF); macrophage stimulating factor (MSP); Interleukins (IL), such as IL-1, IL-1a, IL-1b, IL-1RA, IL-18, IL-2, IL-3, IL-4, IL-5, IL-6, IL-7; IL-8, IL-9, IL-10, IL-11, IL-12, IL-12b, IL-13, IL-14, IL-15, IL-16, IL-17, IL-20; tumor necrosis factors such as CD154, LT-beta, TNF-alpha, TNF-beta, 4-1BBL, APRIL, CD70, CD153, CD178, GITRL, LIGHT, OX40L, TALL-1, TRAIL, TWEAK, TRANCE; and other polypeptide factors such as LIF and oncostatin M (OSM) and kit ligand (KL). Cytokine receptor refers to a receptor protein that binds cytokines. Cytokine receptors can be membrane bound and soluble.

A target polynucleotide may encode a cytokine. Non-limiting examples of cytokines are 4-1BBL, activin βA, activin βB, activin βC, activin βE, artemin (ARTN), BAFF/BLyS/TNFSF138, BMP10, BMP15, BMP2, BMP3, BMP4 , BMP5, BMP6, BMP7, BMP8a, BMP8b, bone morphogenetic protein 1 (BMP1), CCL1/TCA3, CCL11, CCL12/MCP-5, CCL13/MCP-4, CCL14, CCL15, CCL16, CCL17/TARC, CCL18, CCL19, CCL2/MCP-1, CCL20, CCL21, CCL22/MDC, CCL23, CCL24, CCL25, CCL26, CCL27, CCL28, CCL3, CCL3L3, CCL4, CCL4L1/LAG-1, CCL5, CCL6, CCL7, CCL8, CCL9, CD153/CD30L/TNFSF8, CD40L/CD154/TNFSF5, CD40LG, CD70, CD70/CD27L/TNFSF7, CLCF1, c-MPL/CD110/ TPOR, CNTF, CX3CL1, CXCL1, CXCL10, CXCL11, CXCL12, CXCL13, CXCL14, CXCL15, CXCL16, CXCL17, CXCL2/MIP-2, CXCL3, CXCL4, CXCL5, CXCL6, CXCL7/Ppbp, CXCL9, EDA-A1, FAM19A1, FAM19A2, FAM19A3, FAM19A4, FAM19A5, Fas ligand/FASLG/CD95L/CD178, GDF10, GDF11 , GDF15, GDF2, GDF3, GDF4, GDF5, GDF6, GDF7, GDF8, GDF9, glial cell line-derived neurotrophic factor (GDNF), growth differentiation factor 1 (GDF1), IFNA1, IFNA10, IFNA13, IFNA14, IFNA2, IFNA4 , IFNA5/IFNaG, IFNA7, IFNA8, IFNB1, IFNE, IFNG, IFNZ, IFNω/IFNW1, IL11, IL18, IL18BP, IL1A, IL1B, IL1F10, IL1F3/IL1RA, IL1F5, IL1F6, IL1F7, IL1F8, IL1F9, IL1RL2, IL31 , IL33, IL6, IL8/CXCL8, inhibin-A, inhibin-B, leptin, LIF, LTA/TNFB/TNFSF1, LTB/TNFC, neurturin; NRTN), OSM, OX-40L/TNFSF4/CD252, persepin (PSPN), RANKL/OPGL/TNFSF11 (CD254), TL1A/TNFSF15, TNFA, TNF-alpha/TNFA, TNFSF10/TRAIL/APO-2L ( CD253), TNFSF12, TNFSF13, TNFSF14/LIGHT/CD258, XCL1, and XCL2. In some embodiments, the target gene encodes an immune checkpoint inhibitor. Non-limiting examples of such immune checkpoint inhibitors include PD-1, CTLA-4, LAG3, TIM-3, A2AR, B7-H3, B7-H4, BTLA, IDO, KIR and VISTA. In some embodiments, the target gene encodes a T cell receptor (TCR) alpha, beta, gamma and/or delta chain.

In some cases, a cytokine may be a chemokine. The chemokines are ARMCX2, BCA-1/CXCL13, CCL11, CCL12/MCP-5, CCL13/MCP-4, CCL15/MIP-5/MIP-1 Delta, CCL16/HCC-4/NCC4, CCL17/TARC, CCL18/PARC /MIP-4, CCL19/MIP-3b, CCL2/MCP-1, CCL20/MIP-3 alpha/MIP3A, CCL21/6Ckine, CCL22/MDC, CCL23/MIP 3, CCL24/Eotaxin-2/MPIF-2, CCL25/TECK, CCL26/Eotaxin-3, CCL27/CTACK, CCL28, CCL3/Mip1a, CCL4/MIP1B, CCL4L1/LAG-1, CCL5/RANTES, CCL6/C10, CCL8/MCP-2, CCL9, CML5, CXCL1 , CXCL10/Crg-2, CXCL12/SDF-1 Beta, CXCL14/BRAK, CXCL15/Lungkine, CXCL16/SR-PSOX, CXCL17, CXCL2/MIP-2, CXCL3/GRO Gamma, CXCL4/PF4, CXCL5, CXCL6/GCP -2, CXCL9/MIG, FAM19A1, FAM19A2, FAM19A3, FAM19A4/TAFA4, FAM19A5, Fractalkine/CX3CL1, I-309/CCL1/TCA-3, IL-8/CXCL8, MCP-3/CCL7, NAP -2/PPBP/CXCL7, XCL2 and IL10, but not limited thereto.

Table 3g provides a non-limiting list of such BP sequences included in the compositions of the present disclosure. In some embodiments of the compositions disclosed herein, where the biologically active moiety can be a biologically active peptide (BP), the BP has at least (about) 80% sequence identity (e.g., For example, at least (about) 81%, at least (about) 82%, at least (about) 83%, at least (about) 84%, at least (about) 85%, at least (about) 86%, at least (about) 87% , at least (about) 88%, at least (about) 89%, at least (about) 90%, at least (about) 91%, at least (about) 92%, at least (about) 93%, at least (about) 94%, at least (about) 95%, at least (about) 96%, at least (about) 97%, at least (about) 98%, at least (about) 99%, or 100% sequence identity). there is.

Table 3g. Cytokines for conjugation

“IL-1ra” refers to the human IL-1 receptor antagonist protein and its species and sequence variants, including anakinra (Kineret®), a sequence variant that has at least some of the biological activity of mature IL-1ra. Human IL-1ra is a mature glycoprotein composed of 152 amino acid residues. The inhibitory action of IL-1ra occurs due to binding to the type I IL-1 receptor. This protein has an intrinsic molecular weight of 25 kDa, and this molecule shows limited sequence homology to IL-1α (19%) and IL-1ß (26%). Anakinra is an unglycosylated, recombinant human IL-1ra and differs from endogenous human IL-1ra by the addition of an N-terminal methionine. A commercialized version of anakinra is marketed as Kineret®. It binds to the IL-1 receptor with the same avidity as native IL-1ra and IL-1b, but there is only one receptor-binding motif on IL-1ra compared to these two motifs on IL-1α and IL-1ß. It does not cause receptor activation (signal transduction), which is the effect that occurs by doing so. Anakinra is reported to have 153 amino acids, a size of 17.3 kD, and a half-life of approximately 4-6 hours.

various viral, bacterial, fungal and parasitic infections; intravascular coagulation; high-dose IL-2 therapy; solid tumor; leukemia; Alzheimer's disease; HIV-1 infection; autoimmune disorders; trauma (surgery); hemodialysis; ischemic disease (myocardial infarction); noninfectious hepatitis; asthma; UV irradiation; closed head injury; pancreatitis; peritonitis; graft versus host disease; patients with transplant rejection; and increased IL-1 production in healthy subjects after excessive exercise. It has been associated with increased IL-1b production in Alzheimer's disease patients, and there is a possible role for IL1 in the release of amyloid precursor protein. IL-1 is also found in type 2 diabetes, obesity, hyperglycemia, hyperinsulinemia, type 1 diabetes, insulin resistance, retinal neurodegenerative processes, disease states and conditions characterized by insulin resistance, acute myocardial infarction (AMI), acute Coronary artery syndrome (ACS), atherosclerosis, chronic inflammatory disorders, rheumatoid arthritis, degenerative intervertebral disc disease, sarcoidosis, Crohn's disease, ulcerative colitis, gestational diabetes, excessive appetite, insufficient satiety, metabolic disorders, glucagonoma, airway Secretory disorders, osteoporosis, central nervous system disease, restenosis, neurodegenerative diseases, renal failure, congestive heart failure, renal syndrome, liver cirrhosis, pulmonary edema, hypertension, disorders in which reduced food intake is desirable, irritable bowel syndrome, myocardial infarction, stroke, surgery Post-catabolic changes, hibernating heart muscle, diabetic cardiomyopathy, insufficient urinary sodium excretion, excessive urinary potassium concentration, toxic hypervolemia-related conditions or disorders, polycystic ovarian syndrome, dyspnoea, chronic skin ulcers, nephropathy, left ventricular systolic function Disorders, Gastrointestinal Diarrhea, Postoperative Dumping Syndrome, Irritable Bowel Syndrome, Majority Disease Polyneuropathy (CIPN), Systemic Inflammatory Response Syndrome (SIRS), Dyslipidemia, Post-Ischemic Reperfusion Injury and Coronary Heart Disease Risk Factor (CHDRF) associated with diseases such as syndrome. The IL-1ra containing fusion proteins of the present invention may find particular use in the treatment of any of the diseases and disorders described above. IL-1ra was cloned as described in US Pat. Nos. 5,075,222 and 6,858,409.

In some cases, BP may be IL-10. IL-10 may be an effective anti-inflammatory cytokine that inhibits the production of pro-inflammatory cytokines and chemokines. IL-10 is one of the major TH2 type cytokines that increase the humoral immune response and lower the cell-mediated immune response. IL-10 may be useful in the treatment of autoimmune and inflammatory diseases such as rheumatoid arthritis, multiple sclerosis, myasthenia gravis, systemic lupus erythematosus, Alzheimer's disease, schizophrenia, allergic asthma, retinal neurodegenerative processes and diabetes.

In some cases, IL-10 can be modified to improve stability and reduce pyrolytic degradation. The modification may be one or more amide bond substitutions. In some cases, replacing one or more amide linkages in the backbone of IL-10 can achieve the above-mentioned effects. One or more amide linkages (-CONH-) of IL-10 can be replaced with linkages that are isoforms of the amide linkages:

-CH ₂ NH-, -CH ₂ S-, -CH ₂ CH ₂ -, -CH=CH- (cis and trans), -COCH ₂ -, -CH(OH)CH ₂ - or -CH ₂ SO-. Furthermore, the amide linkage of IL-10 may be replaced with a reduced isosteric pseudopeptide linkage. See Couder et al. (1993) Int. J. Peptide Protein Res. 41:181-184, which is incorporated herein by reference in its entirety).

one or more acidic amino acids including aspartic acid, glutamic acid, homoglutamic acid, tyrosine, alkyl, aryl, arylalkyl and heteroaryl sulfonamides of 2,4-diaminopripyionic acid, ornithine or lysine and tetrazole substituted alkyl amino acids ; and side chain amide residues such as asparagine, glutamine, and alkyl or aromatic substituted derivatives of asparagine or glutamine; In addition, hydroxyl-containing amino acids may be substituted, including serine, threonine, homoserine, 2,3-diaminopropionic acid, and alkyl or aromatic substituted derivatives of serine or threonine.

One or more hydrophobic amino acids of IL-10, such as alanine, leucine, isoleucine, valine, norleucine, (S)-2-aminobutyric acid, (S)-cyclohexylalanine or other simple alpha-amino acids, can be branched, cyclic and straight chain It may be substituted with amino acids, including but not limited to, aliphatic side chains of C1 to C10 carbons containing alkyl, alkenyl or alkynyl substitutions.

In some cases, one or more hydrophobic amino acids in IL-10 may be substituted, such as phenylalanine, tryptophan, tyrosine, sulfotyrosine, biphenylalanine, 1-naphthylalanine, 2-naphthylalanine, 2-benzothienylalanine , 3-benzothienylalanine, histidine (amino, alkylamino, dialkylamino, aza, halogenated (fluoro, chloro, bromo or iodo) or alkoxy (from C ₁ -C ₄ of the aromatic amino acids listed above) substitutions of aromatic substituted hydrophobic amino acids, including substituted forms), illustrative examples of which are: 2-, 3- or 4-aminophenylalanine, 2-, 3- or 4-chlorophenylalanine, 2 -, 3- or 4-methylphenylalanine, 2-, 3- or 4-methoxyphenylalanine, 5-amino-, 5-chloro-, 5-methyl- or 5-methoxytryptophan, 2'-, 3'- , or 4'-amino-, 2'-, 3'-, or 4'-chloro-, 2, 3, or 4-biphenylalanine, 2'-, 3'- or 4'-methyl-, 2-, 3- or 4-biphenylalanine and 2- or 3-pyridylalanine.

One or more hydrophobic amino acids in IL-10, such as phenylalanine, tryptophan, tyrosine, sulfotyrosine, biphenylalanine, 1-naphthylalanine, 2-naphthylalanine, 2-benzothienylalanine, 3-benzothienylalanine, histidine ( amino, alkylamino, dialkylamino, aza, halogenated (including fluoro, chloro, bromo or iodo) or alkox) may be substituted with aromatic amino acids including: 2-, 3- or 4- Aminophenylalanine, 2-, 3- or 4-chlorophenylalanine, 2-, 3- or 4-methylphenylalanine, 2-, 3- or 4-methoxyphenylalanine, 5-amino-, 5-chloro-, 5-methyl - or 5-methoxytryptophan, 2'-, 3'-, or 4'-amino-, 2'-, 3'-, or 4'-chloro-, 2, 3, or 4-biphenylalanine, 2' -, 3'- or 4'-methyl-, 2-, 3- or 4-biphenylalanine and 2- or 3-pyridylalanine

Amino acids with basic side chains including arginine, lysine, histidine, ornithine, 2,3-diaminopropionic acid, homoarginine (including alkyl, alkenyl or aryl substituted derivatives of the aforementioned amino acids) may be substituted. Examples are N-epsilon-isopropyl-lysine, 3-(4-tetrahydropyridyl)-glycine, 3-(4-tetrahydropyridyl)-alanine, N,N-gamma, gamma'-diethyl-homo arginine, alpha-methyl-arginine, alpha-methyl-2,3-diaminopropionic acid, alpha-methyl-histidine and alpha-methyl-ornithine, wherein the alkyl group occupies the pro-R position of the alpha-carbon. Modified IL-10 is an amide or acid chloride formed from any combination of alkyl, aromatic, heteroaromatic, ornithine or 2,3-diaminopropionic acid, carboxylic acid, active ester, active azolide and related derivatives, lysine and any of a number of well-known activated derivatives such as ornithine.

In some cases, IL-10 may include one or more naturally occurring L-amino acids, synthetic L-amino acids, and/or D-enantiomers of amino acids. An IL-10 polypeptide may comprise one or more of the following amino acids: ω-aminodecanoic acid, ω-aminotetradecanoic acid, cyclohexylalanine, α,γ-diaminobutyric acid, α,β-diaminopropionic acid, δ -Aminovaleric acid, t-butylalanine, t-butylglycine, N-methylisoleucine, phenylglycine, cyclohexylalanine, norleucine, naphthylalanine, ornithine, citrulline, 4-chlorophenylalanine, 2-fluorophenylalanine, Pyridylalanine 3-benzothienyl alanine, hydroxyproline, β-alanine, o-aminobenzoic acid, m-aminobenzoic acid, p-aminobenzoic acid, m-aminomethylbenzoic acid, 2,3-diaminopropionic acid, α-amino Isobutyric acid, N-methylglycine (sarcosine), 3-fluorophenylalanine, 4-fluorophenylalanine, penicillamine, 1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid, β-2 -Thienylalanine, methionine sulfoxide, homoarginine, N-acetyllysine, 2,4-diaminobutyric acid, rho-aminophenylalanine, N-methylvaline, homocysteine, homoserine, ε-aminohexanoic acid, ω-aminohexane acids, ω-aminoheptanoic acid, ω-aminooctanoic acid and 2, 3-diaminobutyric acid.

IL-10 can contain cysteine residues, or cysteine, which can act as a linker to another peptide via a disulfide bridge or provide for cyclization of an IL-10 polypeptide. Methods for introducing cysteine or cysteine analogs are known in the art; See, eg, US Patent No. 8,067,532. IL-10 polypeptides can be cyclized. Other means of cyclization include introduction of oxime linkers or lanthionine linkers; See, eg, US Patent No. 8,044,175. Any combination of amino acids (or non-amino acid moieties) capable of forming a cyclization bond may be used and/or introduced. A cyclization bond can be created with any combination of amino acids (or amino acids with -(CH ₂ ) _n CO- or -(CH ₂ ) _n C ₆ H ₄ -CO-) that allows introduction of a bridge. Some examples are disulfide, -(CH ₂ ) _n -carba bridges, thioacetals, disulfide mimics such as thioether bridges (cystathionine or lanthionine) and bridges involving esters and ethers.

IL-10 is N-alkyl, aryl to construct N-terminal modified derivatives including lactams and other ring structures, C-terminal hydroxymethyl derivatives, o-modified derivatives, and substituted amides such as alkylamides and hydrazides. or backbone crosslinks. In some cases, an IL-10 polypeptide is a retroinverso analog.

IL-10 can be a native protein, a peptide fragment IL-10 having at least a portion of the biological activity of native IL-10, or a modified peptide. IL-10 can be modified to improve uptake into cells. One such modification may be the attachment of a protein transduction domain. A protein transduction domain may be attached to the C-terminus of IL-10. Alternatively, the protein transduction domain can be attached to the N-terminus of IL-10. The protein transduction domain may be attached to IL-10 via a covalent bond. Protein transduction domains can be selected from any of the sequences listed in Table 3h .

Table 3h. Exemplary Protein Transduction Domains

The BPs of the compositions of the present invention are not limited to natural, full-length polypeptides, but include recombinant versions as well as biologically and/or pharmacologically active variants or fragments thereof. It will be appreciated that various amino acid substitutions may be made in the GP to generate variants without departing from the spirit of the invention, for example with respect to the biological activity or pharmacological properties of the BP. Examples of conservative substitutions for amino acids in a polypeptide sequence are shown in Table 4 . However, in embodiments of the compositions of the present disclosure in which the sequence identity of the BP is less than 100% compared to a particular sequence disclosed herein, the present invention provides a sequence identity of a given BP, which may be at any position within the sequence of the BP, including contiguous amino acid residues. Substitutions of any of the other 19 natural L-amino acids for a given amino acid residue are contemplated. Where any one substitution results in an undesirable change in biological activity, one of the replacement amino acids may be used and by the methods described herein or, for example, in U.S. Patent No. 5,364,934 (see, in its entirety Constructs can be evaluated using any of the techniques and guidelines for conservative and non-conservative mutations set forth in), or using methods generally known to those skilled in the art. Variants may also include, for example, polypeptides in which one or more amino acid residues are added or deleted at the N- or C-terminus of the full-length native amino acid sequence of the BP that retains at least a portion of the biological activity of the native peptide.

Table 4 Exemplary Conservative Amino Acid Substitutions

In some embodiments, the BP incorporated into the compositions of the present disclosure is at least (about) 80% (or at least (about) 81%, or at least (about) 82%, or at least (about) the sequences of Tables 3a-3h 83%, or at least (about) 84%, or at least (about) 85%, or at least (about) 86%, or at least (about) 87%, or at least (about) 88%, or at least (about) 89% , or at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99%, or (about) 100% sequence identity. In some embodiments of the composition of the disclosure, the sequence of BP may include one or more substitutions shown in Table 4 .

Antibodies:

In some embodiments of the compositions of the present disclosure, the biologically active peptide (BP) may include an antibody, such as a monospecific, bispecific or multispecific antibody. An antibody may comprise a binding domain (or binding moiety) that has a specific binding affinity for a tumor specific marker or antigen of a target cell (or target cell antigen) (eg, as described more fully below). there is. An antibody may include a binding domain (or binding moiety) that binds an effector cell antigen ( eg, as described more fully below ). In some embodiments of the compositions of the present disclosure, the antibody, such as a bispecific or multispecific antibody, is specific for (1) a tumor specific marker or target cell antigen (eg, as described more fully below) (2) another binding domain (e.g., a first or second binding domain) that binds an effector cell antigen ( e.g., as described more fully below ) with binding affinity; , a second or first binding domain). The present disclosure relates to single chain binding domains such as, but not limited to, Fv, Fab, Fab', Fab'-SH, Nanobodies (also known as single domain antibodies or V _HH ), F(ab')2 , linear antibodies, single domain antibodies, single domain camelid antibodies, single chain antibody molecules (scFv), multispecific antibodies formed from antibody fragments, and diseased tissues or cells (eg, cancer, tumors, or other malignant tissues) The use of diabodies capable of binding ligands or receptors associated with effector cells and antigens of the present invention is contemplated. The binding domain (or first binding domain, or second binding domain) can be a non-antibody scaffold selected from anticalins, adnectins, pynomers, affilins, affibodies, centrins, and DARPins. The binding domain (or first binding domain, or second binding domain) to a tumor cell target is a T cell receptor engineered to bind to a major histocompatibility complex (MHC) loaded with a peptide fragment of a protein overexpressed by the tumor cell. It can be a variable domain. In some embodiments of the compositions of the present disclosure (e.g., XTENylated protease activated T cell engagers (“XPAT” or “XPATs”), other masked therapeutic antibodies, etc.), the biologically active peptide (BP) is a bispecific an antibody (eg, a bispecific T cell engager).

As is well established with respect to single chain binding domains (or binding moieties), an active antibody fragment (Fv) is the smallest antibody fragment that contains a complete antigen recognition and binding site, one heavy chain (VH) and one heavy chain (VH) in non-covalent association. It consists of a dimer of the light chain variable domain (VL) of Each scFv may include one VL and one VH. Within each VH and VL chain there are three complementarity determining regions (CDRs) that interact to define the antigen binding site on the surface of the VH-VL dimer; The six CDRs of the binding domain (or binding moiety) confer antigen binding specificity to the antibody or single chain binding domain (or binding moiety). In some cases, scFvs are created with 3, 4 or 5 CHRs in each binding domain (or binding moiety), respectively. The framework sequences flanking the CDRs have tertiary structures that are essentially conserved in native immunoglobulins across species, and the framework residues (FRs) are responsible for keeping the CDRs in proper orientation. Constant domains are not required for binding function, but may help stabilize VH-VL interactions. In some embodiments, the domains of the binding site of a polypeptide may be a pair of VH-VL, VH-VH or VL-VL domains of either the same or different immunoglobulins, but generally each VH and VL chain from a parent antibody. It is preferred to use to make a single chain binding domain (or binding moiety). The order of the VH and VL domains within the polypeptide chain is not limiting for the present invention; It is understood that the VH and VL domains are arranged such that the antigen binding site is properly folded, although the order of a given domain can generally be reversed without loss of function. Thus, the single chain binding domains of the bispecific scFv embodiments of the subject composition may be in the order (VL-VH)1-(VL-VH)2, where “1” and “2” represent the first and second bonds, respectively. domain (or first and second binding moieties)), or (VL-VH)1-(VH-VL)2, or (VH-VL)1-(VL-VH)2, or (VH- VL)1-(VH-VL)2, wherein the paired binding domains (or binding moieties) are linked by a polypeptide linker as described below.

Thus, BP binds to (1) a binding domain (or binding moiety) with specific binding affinity for a tumor-specific marker or antigen of a target cell (or target cell antigen) and (2) binding to an effector cell antigen. In some embodiments of the composition comprising a domain (or binding moiety), the arrangement of binding domains (or binding moieties) in an exemplary bispecific single chain antibody disclosed herein is a first binding domain (or first binding moiety). T) may be located C-terminal to the second binding domain (or second binding moiety). The arrangement of the V chain is VH (target cell surface antigen) -VL (target cell surface antigen) -VL (effector cell antigen) -VH (effector cell antigen), VH (target cell surface antigen) -VL (target cell surface antigen) -VH (effector cell antigen) -VL (effector cell antigen), VL (target cell surface antigen) -VH (target cell surface antigen) -VL (effector cell antigen) -VH (effector cell antigen) or VL (target cell surface antigen) antigen)-VH (target cell surface antigen)-VH (effector cell antigen)-VL (effector cell antigen). For arrangements in which the second binding domain (or second binding moiety) can be positioned N-terminal to the first binding domain (or first binding moiety), the following sequence is possible: VH (effector cell antigen) )-VL (effector cell antigen)-VL (target cell surface antigen)-VH (target cell surface antigen), VH (effector cell antigen)-VL (effector cell antigen)-VH (target cell surface antigen)-VL (target cell surface antigen), VL (effector cell antigen)-VH (effector cell antigen)-VL (target cell surface antigen)-VH (target cell surface antigen) or VL (effector cell antigen)-VH (effector cell antigen)-VH (Target Cell Surface Antigen)-VL (Target Cell Surface Antigen). As used herein, “at the N-terminus of” or “at the C-terminus of” and grammatical variations thereof refer to within the primary amino acid sequence rather than placement at the absolute N- or C-terminus of the bispecific single chain antibody. Indicates relative position. Thus, as a non-limiting example, a first binding domain (or first binding moiety) that is “located C-terminal to the second binding domain” means that the first binding occurs within a bispecific single chain antibody to a second binding domain. (or the second binding moiety), and an additional sequence, such as a His-tag or another compound such as a radioactive isotope, may be located at the C-terminus of the bispecific single chain antibody. Do not rule out the possibility.

The VL and VH domains may be derived from monoclonal antibodies with binding specificities for tumor specific markers or antigens of target cells and effector cell antigens, respectively. In other cases, the first and second binding domains (or first and second binding moieties) are each of six regions derived from a monoclonal antibody having binding specificity for a target cell marker, such as a tumor specific marker and an effector cell antigen. Each contains a CDR. In other embodiments, the first and second binding domains (or first and second binding moieties) of a subject composition may have 3, 4 or 5 CHRs within each binding domain (or each binding moiety). there is. In another embodiment, an embodiment of the invention provides a first binding domain comprising a CDR-H1 region, a CDR-H2 region, a CDR-H3 region, a CDR-L1 region, a CDR-L2 region, and a CDR-H3 region, respectively; and and a second binding domain, wherein each domain may be derived from a monoclonal antibody capable of binding a tumor specific marker or antigen of a target cell and an effector cell antigen, respectively.

In some embodiments, where the BP comprises a binding domain (or binding moiety) (or first binding domain, or second binding domain) that has binding affinity for an effector cell antigen, the effector cell antigen is a plasma cell; can be expressed on the surface of effector cells selected from T cells, B cells, cytokine induced killer cells (CIK cells), mast cells, dendritic cells, regulatory T cells (RegT cells), helper T cells, myeloid cells and NK cells. there is. Effector cell antigens can be expressed on or within effector cells. Effector cell antigens can be expressed on T cells such as CD4+, CD8+ or natural killer (NK) cells. Effector cell antigens can be expressed on the surface of T cells. Effector cell antigens can be expressed on B cells, mast cells, dendritic cells or myeloid cells.

In some embodiments of the compositions herein, the BP is a binding domain (or binding moiety) having a specific binding affinity for a tumor specific marker or antigen of a target cell (or target cell antigen) (or a first binding domain, or a second binding domain). Tumor specific markers or target cell antigens can be associated with tumor cells. Tumor cells may be cells of a tumor, such as a stromal cell tumor, a fibroblast tumor, a myofibroblast tumor, a glial cell tumor, an epithelial cell tumor, an adipocyte tumor, an immune cell tumor, a vascular cell tumor, or a smooth muscle cell tumor. Tumor-specific markers or antigens of target cells include alpha 4 integrin, Ang2, B7-H3, B7-H6 (eg, its natural ligand Nkp30, which is not an antibody fragment), CEACAM5, cMET, CTLA4, FOLR1, EpCAM, CCR5, CD19, HER2, HER2 neu, HER3, HER4, HER1 (EGFR), PD-L1, PSMA, CEA, TROP-2, MUC1 (mucin), MUC-2, MUC3, MUC4, MUC5AC, MUC5B, MUC7, MUC16 βhCG, Lewis-Y, CD20, CD33, CD38, CD30, CD56 (NCAM), CD133, ganglioside GD3; 9-O-Acetyl-GD3, GM2, Globo H, Fucosyl GM1, GD2, Carbonic Anhydrase IX, CD44v6, Nectin-4, Sonic Hedgehog (Shh), Wue-1, Plasma Cell Antigen 1, melanoma chondroitin sulfate proteoglycan (MCSP), CCR8, 6-dural epithelial antigen of the prostate (STEAP), mesothelin, A33 antigen, prostate stem cell antigen (PSCA), Ly-6, desmoglein 4, fetal acetyl Choline Receptor (fnAChR), CD25, Cancer Antigen 19-9 (CA19-9), Cancer Antigen 125 (CA-125), Müller Inhibitor Receptor Type II (MISIIR), Sialated Tn Antigen (sTN), Fibroblast Activating Antigen (FAP), endosialin (CD248), epidermal growth factor receptor variant III (EGFRvIII), tumor-associated antigen L6 (TAL6), SAS, CD63, TAG72, Thomsen-Friedenreich antigen (TF-antigen), insulin-like growth factor I Receptor (IGF-IR), Cora antigen, CD7, CD22, CD70 (e.g. natural ligand, not an antibody fragment, CD27), CD79a, CD79b, G250, MT-MMP, CA19-9, CA-125 , alpha-fetoprotein (AFP), VEGFR1, VEGFR2, DLK1, SP17, ROR1 and EphA2. Tumor specific markers or antigens of target cells are alpha 4 integrin, Ang2, B7-H3, B7-H6 (e.g. its natural ligand Nkp30 which is not an antibody fragment), CEACAM5, cMET, CTLA4, FOLR1, EpCAM (epithelial cell adhesion molecule), CCR5, CD19, HER2, HER2 neu, HER3, HER4, HER1 (EGFR), PD-L1, PSMA, CEA, TROP-2, MUC1 (mucin), MUC-2, MUC3, MUC4, MUC5AC, MUC5B , MUC7, MUC16 βhCG, Lewis-Y, CD20, CD33, CD38, CD30, CD56 (NCAM), CD133, ganglioside GD3, 9-O-acetyl-GD3, GM2, Globo H, Fucosyl GM1, GD2, Carbonic Anhydrase IX, CD44v6, Nectin-4, Sonic Hedgehog (Shh), Wue-1, Plasma Cell Antigen 1 (PC-1), Melanoma Chondroitin Sulfate Proteoglycan (MCSP), CCR8, prostate 6-dural epithelial antigen (STEAP), mesothelin, A33 antigen, prostate stem cell antigen (PSCA), Ly-6, desmoglein 4, fetal acetylcholine receptor (fnAChR), CD25, cancer antigen 19- 9 (CA19-9), cancer antigen 125 (CA-125), Müller inhibitor receptor type II (MISIIR), sialylated Tn antigen (sTN), fibroblast activating antigen (FAP), endosialin (CD248), epidermal Growth factor receptor variant III (EGFRvIII), tumor-associated antigen L6 (TAL6), SAS, CD63, TAG72, Thomsen-Friedenreich antigen (TF-antigen), insulin-like growth factor I receptor (IGF-IR), Cora antigen , CD7, CD22, CD70 (e.g., a natural ligand that is not an antibody fragment, CD27), CD79a, CD79b, G250, MT-MMP, alpha-fetoprotein (AFP), VEGFR1, VEGFR2, DLK1, SP17, ROR1, EphA2 , ENPP3, glypican 3 (GPC3) and TPBG/5T4 (trophoblast glycoprotein). Tumor-specific markers or antigens of target cells include alpha 4 integrin, Ang2, CEACAM5, cMET, CTLA4, FOLR1, EpCAM (epithelial cell adhesion molecule), CD19, HER2, HER2 neu, HER3, HER4, HER1 (EGFR), PD- L1, PSMA, CEA, TROP-2, MUC1 (mucin), Lewis-Y, CD20, CD33, CD38, mesothelin, CD70 (eg, its natural ligand, not an antibody fragment, CD27), VEGFR1, VEGFR2, ROR1 , EphA2, ENPP3, Glypican 3 (GPC3) and TPBG/5T4 (trophoblast glycoprotein). The VL and VH sequences of a binding domain (or binding moiety) (or first binding domain, or second binding domain) having specific binding affinity for a tumor-specific marker or antigen of a target cell (or target antigen) at least (about) 90%, or at least (about) 91%, of any one of the paired VL and VH sequences set forth in the "VH Sequences" and "VL Sequences" columns of Table 6 (as described more fully below); or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99%, or 100% sequence identity.

Therapeutic monoclonal antibodies for a subject composition from which the VL and VH and CDR domains may be derived are known in the art. Such therapeutic antibodies include rituximab, IDEC/Genentech/Roche, a chimeric anti-CD20 antibody used in the treatment of many lymphomas, leukemias, and some autoimmune disorders (see, eg, US Pat. No. 5,736,137); ofatumumab, an anti-CD20 antibody in development by GlaxoSmithKline, approved for use in chronic lymphocytic leukemia and in development for follicular non-Hodgkin's lymphoma, diffuse large B-cell lymphoma, rheumatoid arthritis and relapsing-remitting multiple sclerosis; Lukatumumab (HCD122), an anti-CD40 antibody developed by Novartis for non-Hodgkin's or Hodgkin's lymphoma (see, eg, US Pat. No. 6,899,879), binds to cells expressing CD20 to treat non-Hodgkin's lymphoma AME-133, an antibody developed by Applied Molecular Evolution to treat antibody-immune thrombocytopenic purpura; Beltuzumab (hA20), an antibody developed by Immunomedics, Inc. that binds to cells expressing CD20 to treat antibody-immune thrombocytopenic purpura; low-grade B cells HumaLYM developed by Intracel for the treatment of lymphoma and ocrelizumab developed by Genentech, an anti-CD20 monoclonal antibody for the treatment of rheumatoid arthritis (see e.g. US Patent Application 20090155257), developed by Genentech, approved for the treatment of breast cancer trastuzumab, a humanized anti-Her2/neu antibody (see, eg, US Pat. No. 5,677,171); Pertuzumab, an anti-HER2 dimerization inhibitor antibody developed by Genentech for the treatment of prostate, breast and ovarian cancer; (See eg US Patent No. 4,753,894); Cetuximab, an anti-EGFR antibody used in the treatment of epidermal growth factor receptor (EGFR) expressing, KRAS wild-type metastatic colorectal and head and neck cancers, developed by Imclone and BMS (U.S. Patent No. 4,943,533; see PCT WO 96/40210) ; panitumumab, a fully human monoclonal antibody specific for the epidermal growth factor receptor (also known as the EGF receptor, EGFR, ErbB-1 and HER1), currently marketed by Amgen for the treatment of metastatic colorectal cancer (see US Pat. No. 6,235,883); zalutumumab, a fully human IgG1 monoclonal antibody developed by Genmab, directed against epidermal growth factor receptor (EGFR) for the treatment of squamous cell carcinoma of the head and neck (eg, US Pat. No. 7,247,301); Nimotuzumab, a chimeric antibody to EGFR developed by Biocon, YM Biosciences (Cuba) and Oncosciences (Europe) in the treatment of squamous cell carcinoma of the head and neck, nasopharyngeal cancer, and glioma (e.g., U.S. Pat. No. 5,891,996; U.S. Patent No. 6,506,883); alemtuzumab, a humanized monoclonal antibody to CD52 marketed by Bayer Schering Pharma for the treatment of chronic lymphocytic leukemia (CLL), cutaneous T-cell lymphoma (CTCL) and T-cell lymphoma; muromonab-CD3, an anti-CD3 antibody developed by Ortho Biotech/Johnson & Johnson, used as an immunosuppressive biologic given to reduce acute rejection in organ transplant patients; ibritumomab tiuxetan, an anti-CD20 monoclonal antibody developed by IDEC/Schering AG as a treatment for some forms of B-cell non-Hodgkin's lymphoma; gemtuzumab ozogamicin, an anti-CD33 (p67 protein) antibody linked to the radioisotope-capable, cytotoxic chelator tiuxetan, developed by Celltech/Wyeth, used in the treatment of acute myelogenous leukemia; ABX-CBL, an anti-CD147 antibody developed by Abgenix; ABX-IL8, an anti-IL8 antibody developed by Abgenix, ABX-MA1, an anti-MUC18 antibody developed by Abgenix, Femtumomab (R1549, 90Y-muHMFG1), an anti-MUC1 being developed by Antisoma, Antisoma developed -MUC1 antibody Therex (R1550), AngioMab (AS1405) developed by Antisoma, HuBC-1 developed by Antisoma, Thioplatin (AS1407) developed by Antisoma, anti-alpha-4-beta-1 developed by Biogen (VLA4) and alpha-4-beta-7 antibody ANTEGREN (natalizumab), VLA-1 mAb, an anti-VLA-1 integrin antibody developed by Biogen, anti-lymphotoxin beta receptor (LTBR) antibody developed by Biogen LTBR mAb, CAT-152, an anti-TGF-β2 antibody developed by Cambridge Antibody Technology, J695, an anti-IL-12 antibody developed by Cambridge Antibody Technology and Abbott, anti-TGF-β2 antibody developed by Cambridge Antibody Technology and Genzyme. CAT-192, a β1 antibody, CAT-213, an anti-eotaxin1 antibody developed by Cambridge Antibody Technology, LYMPHOSTAT-B, an anti-Blys antibody developed by Cambridge Antibody Technology and Human Genome Sciences Inc., Cambridge Antibody Technology and Human Genome Sciences Inc. TRAIL-R1mAb, an anti-TRAIL-R1 antibody developed by Genome Sciences, Inc.; HERCEPTIN, an anti-HER receptor family antibody developed by Genentech; anti-tissue factor (ATF), an anti-tissue factor antibody developed by Genentech; XOLAIR (omalizumab), an anti-IgE antibody developed by Genentech; MLN-02 antibody (formerly LDP-02) developed by Genentech and Millennium Pharmaceuticals; HUMAX CD4®, an anti-CD4 antibody developed by Genmab; Tocilizumab and the anti-IL6R antibody developed by Chugai; HUMAX-IL15, an anti-IL15 antibody developed by Genmab and Amgen; HUMAX-Inflam, developed by Genmab and Medarex; HUMAX-Cancer, an anti-heparanase I antibody developed by Genmab and Medarex and Oxford GlycoSciences; HUMAX-Lymphoma developed by Genmab and Amgen, HUMAX-TAC developed by Genmab; IDEC-131, an anti-CD40L antibody developed by IDEC Pharmaceuticals; IDEC-151 (clenoriximab), an anti-CD4 antibody developed by IDEC Pharmaceuticals; IDEC-114, an anti-CD80 antibody developed by IDEC Pharmaceuticals; IDEC-152, an anti-CD23 developed by IDEC Pharmaceuticals; Anti-KDR antibody developed by Imclone; DC101, an anti-flk-1 antibody developed by Imclone; anti-VE cadherin antibody developed by Imclone; CEA-CIDE (labetuzumab), an anti-carcinoembryonic antigen (CEA) antibody developed by Immunomedics; Yervoy (ipilimumab), an anti-CTLA4 antibody developed by Bristol-Myers Squibb for the treatment of melanoma; Lumphocide® (epratuzumab), an anti-CD22 antibody developed by Immunomedics, AFP-Cide developed by Immunomedics; MyelomaCide developed by Immunomedics; LkoCide developed by Immunomedics; ProstaCide developed by Immunomedics; MDX-010, an anti-CTLA4 antibody developed by Medarex; MDX-060, an anti-CD30 antibody developed by Medarex; MDX-070 developed by Medarex; MDX-018 developed by Medarex; Ocidem (IDM-1), an anti-HER2 antibody developed by Medarex and Immuno-Designed Molecules; HUMAX®-CD4, an anti-CD4 antibody developed by Medarex and Genmab; HuMax-IL15, an anti-IL15 antibody developed by Medarex and Genmab; MOR201, an anti-intracellular adhesion molecule-1 (ICAM-1) (CD54) antibody developed by MorphoSys; tremelimumab, an anti-CTLA-4 antibody developed by Pfizer; visilizumab, an anti-CD3 antibody developed by Protein Design Labs; anti-a 5β1 integrins developed by Protein Design Labs; anti-IL-12 developed by Protein Design Labs; ING-1, an anti-Ep-CAM antibody developed by Xoma; and MLN01, an anti-beta2 integrin antibody developed by Xoma; All antibody references foregoing in this section are expressly incorporated herein by reference. Sequences for these antibodies can be obtained from publicly available databases, patents or references.

Methods for determining the binding affinity and/or other biological activity of a subject composition of the present invention may be those disclosed herein or methods generally known in the art. For example, the binding affinity of a binding pair (eg, antibody and antigen), represented by K _d , can be measured by radioactive binding assays, nonradiative binding assays such as fluorescence resonance energy transfer and surface plasmon resonance (SPR, Biacore). and enzyme-linked immunosorbent assay (ELISA), kinetic exclusion assay (KinExA®), reporter gene activity assay, or a variety of suitable assays described in the Examples. For example, an increase in the binding affinity of a subject therapeutic agent (eg, a chimeric polypeptide assembly) truncated to remove a masking moiety compared to a therapeutic agent (eg, a chimeric polypeptide assembly) to which the masking moiety is attached, or Reduction can be determined by measuring the binding affinity of a therapeutic agent (eg, a chimeric polypeptide assembly) to a target binding partner with or without a masking moiety.

Determination of the half-life of a subject therapeutic agent can be performed by a variety of suitable methods. For example, the half-life of a substance can be determined by administering the substance to a subject and periodically taking a biological sample (eg, a biological fluid such as blood or plasma or ascites) to determine the concentration and/or amount of that substance in the sample over time. can be determined by determining The concentration of a substance in a biological sample can be determined using a variety of suitable methods, including enzyme-linked immunosorbent assay (ELISA), reporter gene activity assay, immunoblot, and chromatographic techniques including high pressure liquid chromatography and rapid protein liquid chromatography. . In some cases, a substance may be labeled with a detectable tag, such as a radioactive tag or a fluorescent tag, that may be used to determine the concentration of the substance in a sample (eg, a blood sample, serum sample, or plasma sample). Various pharmacokinetic parameters can then be determined from the results, which can be done using a software package, such as SoftMax Pro software, or using manual calculations known in the art.

In addition, the degree of solubility, structure and stability maintenance can be confirmed by measuring the physicochemical properties of the subject therapeutic agent (eg, chimeric polypeptide assembly composition). The binding properties of the binding domain (or binding moiety) to the ligand, including the binding dissociation constant (K _d , K _on and K _off ), the half-life of dissociation of the ligand-receptor complex, as well as the specificity of the isolated ligand relative to the free ligand. Assays of subject compositions are performed that allow determination of the activity (IC ₅₀ value) of the binding domain (or binding moiety) to inhibit biological activity. The term “IC ₅₀ ” refers to the concentration required to inhibit half the maximal biological response of a ligand agonist and can generally be determined in a competitive binding assay. The term “EC ₅₀ ” refers to the concentration required to achieve half of the maximal biological response of an active agent and is generally determined by ELISA or cell-based assays and/or reporter gene activity assays, including the methods of the Examples described herein. can

anti-CD3 binding domain

The CD3 complex is a group of cell surface molecules that associate with the T cell antigen receptor (TCR) and function in cell surface expression of the TCR and signaling cascade that originates when a peptide:MHC ligand binds to the TCR. Typically, when an antigen binds to a T cell receptor, CD3 signals through the cell membrane and into the cytoplasm inside the T cell. This results in the activation of rapidly dividing T cells to generate new T cells that are primed to attack the specific antigen to which the TCR is exposed. The CD3 complex is composed of the CD3epsilon molecule, along with four other membrane-bound polypeptides (CD3-gamma, -delta, -zeta, and -beta). In humans, CD3-epsilon is encoded by the CD3E gene on chromosome 11. The intracellular domain of each CD3 chain contains an immunoreceptor tyrosine-based activation motif (ITAM) that serves as a nucleation point for intracellular signaling organization upon T cell receptor engagement.

A number of therapeutic strategies target TCR signaling to modulate T cell immunity, especially by means of anti-human CD3 monoclonal antibodies (mAbs), which are widely clinically used in immunosuppressive regimens. CD3-specific mouse mAb OKT3 is the first mAb approved for use in humans (Sgro, C. Side-effects of a monoclonal antibody, muromonab CD3/orthoclone OKT3: bibliographic review. Toxicology 105:23-29, 1995); Transplant (Chatenoud, Clin. Transplant 7:422-430, (1993); Chatenoud, Nat. Rev. Immunol. 3:123-132 (2003); Kumar, Transplant. Proc. 30:1351-1352 (1998)) , is widely used clinically as an immunosuppressive agent in type 1 diabetes and psoriasis Importantly, anti-CD3 mAbs can induce partial T cell signaling and clonal anergy (Smith, JA, Nonmitogenic Anti- CD3 Monoclonal Antibodies Deliver a Partial T Cell Receptor Signal and Induce Clonal Anergy J. Exp. Med. 185:1413-1422 (1997) OKT3 has been described in the literature as a T cell mitogen as well as a potent T cell killer. (Wong, JT. The mechanism of anti-CD3 monoclonal antibodies. Mediation of cytolysis by inter-T cell bridging. Transplantation 50:683-689 (1990)). In particular, Wong's study showed that cross-linking CD3 T cells and target cells By doing so, killing of the target can be achieved, and FcR-mediated ADCC or complement fixation is not required for the bivalent anti-CD3 MAB to lyse the target cells.

OKT3 exhibits mitogenic and T cell killing activity in a time dependent manner, and after initial activation of T cells leading to cytokine release, further administration of OKT3 blocks all known T cell functions later. It is due to this late blockade of T cell function that OKT3 has found such widespread use as an immunosuppressive agent in therapy regimens for the reduction or even elimination of allograft tissue rejection. Other molecules specific to the CD3 molecule are described in Tunnacliffe, Int. Immunol. 1 (1989), 546-50, WO2005/118635 and WO2007/033230 describe anti-human monoclonal CD3 epsilon antibodies, and US Pat. No. 5,821,337 discloses murine anti-CD3 monoclonal Ab UCHT1 (muxCD3, Shalaby J. Exp. Med. A binding domain capable of binding to an epitope of the epsilon chain is disclosed.

Table 5a. Anti-CD3 monoclonal antibody and VH & VL sequences

* Underlined sequences, if present, are CDRs within VL and VH

In some embodiments of the compositions of the present disclosure, the BP may include a binding domain (or binding moiety) (eg an antigen-binding fragment) that has a specific binding affinity for an effector cell antigen. The effector cell antigen is an effector selected from plasma cells, T cells, B cells, cytokine induced killer cells (CIK cells), mast cells, dendritic cells, regulatory T cells (RegT cells), helper T cells, myeloid cells and NK cells. It can be expressed on the surface of cells. Effector cell antigens can be expressed on the surface of T cells. The binding domain (or binding moiety) may have a binding affinity for CD3. In some embodiments, where a binding domain (or binding moiety) has binding affinity for CD3, a binding domain (or binding moiety) may have binding affinity for a member of a CD3 complex, which is in a discrete form. or independently all known CD3 subunits of the CD3 complex in combined form; Examples include CD3 epsilon, CD3 delta, CD3 gamma, CD3 zeta, CD3 alpha and CD3 beta. A binding domain (or binding moiety) with binding affinity for CD3 may have binding affinity for CD3 epsilon, CD3 delta, CD3 gamma, CD3 zeta, CD3 alpha or CD3 beta.

The origin of an antigen-binding fragment contemplated by this disclosure (comprised of a binding domain or binding moiety) may be a naturally occurring antibody or fragment thereof, a non-naturally occurring antibody or fragment thereof, a humanized antibody or fragment thereof, a synthetic antibody or fragment thereof, a hybrid antibodies or fragments thereof, or engineered antibodies or fragments thereof. Methods for generating antibodies against a given target marker are well known in the art. For example, monoclonal antibodies can be made using the hybridoma method first described by Kohler et al., Nature, 256:495 (1975), or can be made by recombinant DNA methods (USA). Patent No. 4,816,567). The structure of antibodies and fragments thereof, the variable regions of the heavy and light chains of antibodies (VH and VL), single chain variable regions (scFv), complementarity determining regions (CDRs), and domain antibodies (dAbs) are well understood. Methods for generating polypeptides having desired antigen-binding fragments with binding affinity for a given antigen are known in the art.

It will be appreciated that use of the term antigen-binding fragment with respect to compositional embodiments disclosed herein is intended to include a portion or fragment of an antibody that retains the ability to bind an antigen that is a ligand of the corresponding intact antibody. In this embodiment, the antigen-binding fragments include CDRs and intervening framework regions, variable or hypervariable regions (VL, VH) of the light and/or heavy chains of the antibody, variable fragments (Fv), Fab' fragments, F(ab' )2 fragment, Fab fragment, single chain antibody (scAb), VHH camelid antibody, single chain variable fragment (scFv), linear antibody, single domain antibody, complementarity determining region (CDR), domain antibody (dAb), BHH or BNAR type It may be, but is not limited to, a single domain heavy chain immunoglobulin, a single domain light chain immunoglobulin, or other polypeptide known in the art that contains a fragment of an antibody capable of binding an antigen. An antigen-binding fragment having CDR-H and CDR-L may be configured in a (CDR-H)-(CDR-L) or (CDR-H)-(CDR-L) direction from N-terminus to C-terminus. there is. The VL and VH of the two antigen-binding fragments may consist of single-chain diabody constructs; For example, the VL and VH of the first and second binding domains (or binding moieties) are configured with linkers of appropriate length so that they can be arranged as a diabody.

Various CD3 binding domains of the present disclosure have been specifically modified to enhance their stability in the polypeptide embodiments described herein. Binding specificity may be determined by complementarity determining regions (CDRs), such as light chain CDRs or heavy chain CDRs. In many cases, binding specificity is determined by the light chain CDRs and the heavy chain CDRs. A given combination of heavy and light chain CDRs provides a given binding pocket that confers greater affinity and/or specificity for the effector cell antigen compared to other reference antigens. Protein aggregation of antibodies continues to be a major issue in development potential and remains a major focus area for antibody production. Antibody aggregation can be triggered by partial unfolding of its domains, followed by monomer-monomer association, followed by nucleation and aggregate growth. Although the aggregation propensity of antibodies and antibody-based proteins can be influenced by external experimental conditions, they are strongly dependent on the intrinsic antibody properties determined by sequence and structure. It is well known that proteins are only slightly stable in the folded state, but it is often not known that most proteins are inherently prone to aggregation in the unfolded or partially unfolded state, so that aggregates are very stable and long-lived. can A decrease in aggregation propensity has also been shown to be accompanied by an increase in expression titer, demonstrating that reduced protein aggregation is beneficial throughout development and may lead to a more efficient pathway to clinical research. In the case of therapeutic proteins, aggregates are a significant risk factor for adverse immune responses in patients and can form through a variety of mechanisms. Controlling aggregation can improve protein stability, manufacturability, attrition rate, safety, formulation, potency, immunogenicity and solubility. Intrinsic properties of proteins, such as size, hydrophobicity, electrostatic charge and charge distribution, play an important role in protein solubility. Low solubility of therapeutic proteins due to surface hydrophobicity has been shown to make formulation development more difficult and can lead to poor biodistribution, undesirable pharmacokinetic behavior and in vivo immunogenicity. Reducing the overall surface hydrophobicity of a candidate monoclonal antibody can also provide benefits and cost savings associated with purification and dosing regimens. Individual amino acids can be identified by structural analysis as contributing to the antibody's aggregation potential, and can be located in CDRs as well as framework regions. In particular, residues can be predicted to have a high risk of causing hydrophobicity problems in a given antibody.

In some embodiments, the invention provides therapeutics comprising binding domain(s) that have binding affinity for T cell antigen(s). In some embodiments, a binding domain with binding affinity for a T cell antigen may include a VL and VH derived from a monoclonal antibody to an antigen of cluster of differentiation 3 T cell receptor (CD3). The binding domain may include VL and VH derived from monoclonal antibodies to CD3epsilon and CD3delta subunits. Monoclonal antibodies to CD3 neu are known in the art. Illustrative, non-limiting examples of VL and VH sequences of monoclonal antibodies to CD3 are set forth in Table 5a . A binding domain with binding affinity for CD3 can include the anti-CD3 VL and VH sequences shown in Table 5a . A binding domain with binding affinity for CD3epsilon can include the anti-CD3epsilon VL and VH sequences shown in Table 5a . A binding domain having a binding affinity for CD3 may comprise VH and VL regions, wherein each VH and VL region is at least (approximately) identical to the paired VL and VH sequences of the huUCHT1 anti-CD3 antibody of Table 5a. 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95%, or at least (about) 96% , or at least (about) 97%, or at least (about) 98%, or at least (about) 99%, or 100% identity. A binding domain having binding affinity for CD3 may include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region, wherein each of the from each of the anti-CD3 VL and VH sequences shown in 5a . A binding domain having binding affinity for CD3 may comprise a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region and a CDR-H3 region, wherein the CDR sequences. A binding domain having binding affinity for CD3 may comprise a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region and a CDR-H3 region, wherein the CDR sequences are RASQDIRNYLN (SEQ ID NO: 489), YTSRLES (SEQ ID NO: 490), QQGNTLPWT (SEQ ID NO: 491), GYSFTGYTMN (SEQ ID NO: 492), LINPYKGVST (SEQ ID NO: 493) and SGYYGDSDWYFDV (SEQ ID NO: 494).

In some embodiments, the disclosure provides a binding domain (or binding moiety) that binds CD3 for incorporation into a composition described herein, and may include CDR-L and CDR-H. The binding domain that binds CD3 may include CDR-H1, CDR-H2 and CDR-H3, each of which is ( independently ) at least 85%, 86%, 87% , 88%, exhibits 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% sequence identity or have identical amino acid sequences. The binding domain that binds CD3 may include CDR-L1, CDR- L2 and CDR-L3, each of which is ( independently ) at least 85%, 86%, 87%, 88%, exhibits 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% sequence identity or have identical amino acid sequences.

In some embodiments, the present disclosure provides a binding domain that binds CD3 for incorporation into a composition described herein and may include a light chain framework region (FR-L) and a heavy chain framework region (FR-H) ( or a binding moiety). The binding domain that binds CD3 is at least 86%, 87%, 88%, 89%, 90 % , 91%, 92%, 93%, 94%, 95%, 96%, may exhibit 97%, 98%, 99% sequence identity or may contain identical FR-L1s. The binding domain that binds CD3 is at least 86%, 87%, 88%, 89%, 90 % , 91%, 92%, 93%, 94%, 95%, 96%, may exhibit 97%, 98%, 99% sequence identity or may contain identical FR-L2s. The binding domain that binds CD3 is at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96 %, may exhibit 97%, 98%, 99% sequence identity or may contain identical FR-L3s. The binding domain that binds CD3 is at least 86%, 87%, 88%, 89%, 90 % , 91%, 92%, 93%, 94%, 95%, 96%, may exhibit 97%, 98%, 99% sequence identity or may contain identical FR-L4s. The binding domain that binds CD3 is at least 86%, 87%, 88%, 89%, 90 % , 91%, 92%, 93%, 94%, 95%, 96%, may exhibit 97%, 98%, 99% sequence identity or may contain identical FR-H1s. The binding domain that binds CD3 is at least 86%, 87%, 88%, 89%, 90 % , 91%, 92%, 93%, 94%, 95%, 96%, may exhibit 97%, 98%, 99% sequence identity or may contain identical FR-H2s. The binding domain that binds CD3 is at least 86%, 87%, 88%, 89%, 90 % , 91%, 92%, 93%, 94%, 95%, 96%, may exhibit 97%, 98%, 99% sequence identity or may contain identical FR-H3s. The binding domain that binds CD3 is at least 86%, 87%, 88%, 89%, 90 % , 91%, 92%, 93%, 94%, 95%, 96%, may exhibit 97%, 98%, 99% sequence identity or may contain identical FR-H4s.

In some embodiments, the present disclosure provides a binding domain (or binding moiety) that binds CD3 for incorporation into a composition described herein, and may include a variable light (VL) chain amino acid sequence and a variable heavy (VH) chain amino acid sequence. ) is provided. Binding domains that bind CD3 are at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97% of the VL sequences shown in Table 5d . , 98%, 99% sequence identity or may contain identical VLs. Binding domains that bind CD3 are at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97% of the VH sequences shown in Table 5d . , 98%, 99% sequence identity or may contain the same VH. Binding domains that bind CD3 are at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97% of the scFv sequences shown in Table 5d . , 98%, 99% sequence identity or may contain identical amino acid sequences.

In some embodiments of the compositions of the present disclosure, the VL and VH of the antigen-binding fragments are hydrophilic amino acids 25, 26, 27, 28, 29, 30, 31, 32, 33, 34 or 35 that have flexible properties when bound together. can be fused by a relatively long linker consisting of In some embodiments, the VL and VH of any scFv embodiment described herein are selected from the sequence GSGEGSEGEGGGEGSEGEGSGEGGEGEGSG (SEQ ID NO: 495), TGSGEGSEGEGGGEGSEGEGSGEGGEGEGSGT (SEQ ID NO: 496), GATPPETGAETESPGETTGGSAESEPPGEG (SEQ ID NO: 497), or GSAAPTAGTTPSASPAPPTGGSSAAGSPST (SEQ ID NO: 498) They may be linked by relatively long linkers of hydrophilic amino acids.

In some embodiments of the compositions of the present disclosure, where the BP comprises a first binding domain (or first binding moiety) and a second binding domain (or second binding moiety), the first and second binding domains (or first and second binding moieties) may be linked together by a short linker of hydrophilic amino acids having 3, 4, 5, 6 or 7 amino acids. The short linker sequence may be selected from the group of sequences SGGGGS (SEQ ID NO: 499), GGGGS (SEQ ID NO: 500), GGSGGS (SEQ ID NO: 501), GGS or GSP. In some embodiments, the present disclosure provides that, after folding, a first domain (VL or VH) pairs with the last domain (VH or VL) to form one scFv, and the intermediate two domains pair to form a first domain (VL or VH). and another scFv in which the second domain as well as the third and last domains are fused together by one of the aforementioned short linkers and the second and third variable domains are fused by one of the aforementioned relatively long linkers. A composition comprising a chain diabody is provided. As will be appreciated by those skilled in the art, the selection of short and relatively long linkers prevents mispairing of adjacent variable domains, resulting in single-chain diabodies comprising the VL and VH of the first antigen-binding fragment and the second antigen-binding fragment. formation of structures can be facilitated.

Table 5b. Exemplary CD3 CDR sequences

Table 5c. Exemplary CD3 FR sequences

Table 5d. Exemplary VL & VH Sequences

Table 5e: Exemplary scFv sequences

Tumor-specific markers or antigens of target cells

In some embodiments of the compositions of the present disclosure, the binding domain (eg, the first binding domain) may have a specific binding affinity for a tumor specific marker or antigen of a target cell. Some embodiments of the compositions of the present disclosure may include another binding domain (eg, a second binding domain) that binds an effector cell antigen. Tumor-specific markers can be associated with tumor cells (eg, stromal cell tumors, fibroblast tumors, myofibroblast tumors, glial cell tumors, epithelial cell tumors, adipocyte tumors, immune cell tumors, vascular cell tumors or smooth muscle cell tumors). there is. Tumor specific markers or antigens of target cells are alpha 4 integrin, Ang2, B7-H3, B7-H6 (e.g. its natural ligand Nkp30 which is not an antibody fragment), CEACAM5, cMET, CTLA4, FOLR1, EpCAM (epithelial cell adhesion molecule), CCR5, CD19, HER2, HER2 neu, HER3, HER4, HER1 (EGFR), PD-L1, PSMA, CEA, TROP-2, MUC1 (mucin), MUC-2, MUC3, MUC4, MUC5AC, MUC5B , MUC7, MUC16 βhCG, Lewis-Y, CD20, CD33, CD38, CD30, CD56 (NCAM), CD133, ganglioside GD3, 9-O-acetyl-GD3, GM2, Globo H, Fucosyl GM1, GD2, Carbonic Anhydrase IX, CD44v6, Nectin-4, Sonic Hedgehog (Shh), Wue-1, Plasma Cell Antigen 1 (PC-1), Melanoma Chondroitin Sulfate Proteoglycan (MCSP), CCR8, prostate 6-dural epithelial antigen (STEAP), mesothelin, A33 antigen, prostate stem cell antigen (PSCA), Ly-6, desmoglein 4, fetal acetylcholine receptor (fnAChR), CD25, cancer antigen 19- 9 (CA19-9), cancer antigen 125 (CA-125), Müller inhibitor receptor type II (MISIIR), sialylated Tn antigen (sTN), fibroblast activating antigen (FAP), endosialin (CD248), epidermal Growth factor receptor variant III (EGFRvIII), tumor-associated antigen L6 (TAL6), SAS, CD63, TAG72, Thomsen-Friedenreich antigen (TF-antigen), insulin-like growth factor I receptor (IGF-IR), Cora antigen , CD7, CD22, CD70 (e.g., a natural ligand that is not an antibody fragment, CD27), CD79a, CD79b, G250, MT-MMP, alpha-fetoprotein (AFP), VEGFR1, VEGFR2, DLK1, SP17, ROR1, EphA2 , ENPP3, glypican 3 (GPC3) and TPBG/5T4 (trophoblast glycoprotein). Tumor-specific markers or antigens of target cells include alpha 4 integrin, Ang2, CEACAM5, cMET, CTLA4, FOLR1, EpCAM (epithelial cell adhesion molecule), CD19, HER2, HER2 neu, HER3, HER4, HER1 (EGFR), PD- L1, PSMA, CEA, TROP-2, MUC1 (mucin), Lewis-Y, CD20, CD33, CD38, mesothelin, CD70 (eg, its natural ligand, not an antibody fragment, CD27), VEGFR1, VEGFR2, ROR1 , EphA2, ENPP3, Glypican 3 (GPC3) and TPBG/5T4 (trophoblast glycoprotein). The tumor specific marker or antigen of the target cell can be any of those shown in the "Target" column of Table 6 . A binding domain having binding affinity for a tumor-specific marker or antigen of a target cell may comprise VH and VL regions, each VH and VL region set forth in the "VH Sequence" and "VL Sequence" columns of Table 6. at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94% of any one of the paired VL and VH sequences , or at least (about) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99%, or 100% sequence identity. there is.

Table 6. Anti-target cell monoclonal antibodies and sequences

* Sequences in underlined & bold are CDRs within VL and VH, if present

Anti-EpCAM (Epithelial Cell Adhesion Molecule) Binding Domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the tumor specific marker EpCAM. The binding domain may include a VL and a VH derived from a monoclonal antibody to EpCAM. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for EpCAM and another binding domain (e.g., having a specific binding affinity for effector cells). can do.

Monoclonal antibodies to EpCAM are known in the art (as described more fully below). Illustrative, non-limiting examples of EpCAM monoclonal antibodies and their VL and VH sequences are set forth in Table 6 . Some embodiments of a binding domain with binding affinity for the tumor specific marker EpCAM may include the anti-EpCAM VL and VH sequences shown in Table 6 . Some embodiments of a binding domain that has binding affinity for the tumor specific marker EpCAM can include VH and VL regions, wherein each VH and VL region is an anti-EpCAM antibody of Table 6 (eg, 4D5MUCB ) at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94% of the paired VL and VH sequences of ), or at least (about) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the tumor specific marker EpCAM include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. can include, wherein each can be derived from each of the VL and VH sequences shown in Table 6 . Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for EpCAM and another binding domain (e.g., having a specific binding affinity for effector cells). can do. In some embodiments of the compositions of the present disclosure, the binding domain specific for EpCAM may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay. The binding domain may be in scFv format. A binding domain may be in the form of a single chain diabody.

nz, M. Side-by-side analysis of five clinically tested anti-EpCAM monoclonal antibodies Cancer Cell International, 10:44-56, 2010). EpCAM 및 CD3에 대해 유도된 이중특이적 항체가 또한 기재되어 있는데, 2종의 하이브리도마 OKT3 및 9.3 중 어느 하나와 EpCAM에 대한 단클론 항체를 생성하는 하이브리도마를 융합시켜 2종의 상이한 이중특이적 항체의 구축하는 것을 포함한다(Mφller, SA, Reisfeld, RA, Bispecific-monoclonal-antibody-directed lysis of ovarian carcinoma cells by activated human T lymphocytes. Cancer Immunol. Immunother. 33:210-216, 1991). EpCAM에 대한 이중특이적 항체의 다른 예는 BiUII, (항-CD3(래트) x 항-EpCAM(마우스))(Zeidler, J. Immunol., 1999, 163:1247-1252), scFv CD3/17-1A-이중특이적(Mack, M. A small bispecific antibody composition expressed as a functional single-chain molecule with high tumor cell cytotoxicity. Proc. Natl. Acad. Sci., 1995, 92:7021-7025), 및 항-CD3 및 항EpCAM 특이성을 갖는 부분적으로 인간화된 이중특이적 디아바디(Helfrich, W. Construction and characterization of a bispecific diabody for retargeting T cells to human carcinomas. Int. J. Cancer, 1998, 76:232-239)를 포함한다.In general, epithelial cell adhesion molecule (EpCAM, also called 17-1A antigen) is a 40 kDa membrane-integrated glycoprotein composed of 314 amino acids that is expressed in certain epitheliums and many human carcinomas (Balzar, The biology of the 17-1A antigen). 1A antigen (Ep-CAM), see J. Mol. Med. 1999, 77, 699-712). EpCAM was first discovered by the use of the murine monoclonal antibody 17-1A/edrecolomab generated by immunization of mice bearing colon carcinoma cells (Goettlinger, Int J Cancer. 1986; 38, 47-53 and Simon, Proc. Natl. Acad. Sci. USA. 1990, 87, 2755-2759). Because of their epithelial cell origin, most primary, metastatic and disseminated non-small cell lung carcinoma cells. Int. J. Cancer 87(4):548-552, 2000), Martin, IG, Expression of the 17-1A antigen in gastric and gastro-oesophageal junction adenocarcinomas: a potential immunotherapeutic target? J Clin Pathol 1999;52:701-704), and breast and colorectal cancer (Packeisen J, et al. Detection of surface antigen 17-1A in breast and colorectal cancer. Hybridoma. 1999 18(1):37-40). Thus, tumor cells from most carcinomas express EpCAM on their surface (more than normal healthy cells) and are therefore attractive targets for immunotherapeutic approaches. Moreover, increased expression of EpCAM correlates with increased epithelial proliferation, and in breast cancer, overexpression of EpCAM on tumor cells is a predictor of survival (Gastl, Lancet. 2000, 356, 1981-1982). Due to their epithelial cell origin, most carcinoma-derived tumor cells still express EpCAM on their surface, and bispecific solitomab single-chain antibody compositions that target EpCAM on tumor cells and also contain a CD3 binding region can be used as primary Its use on uterine and ovarian CS cell lines has been proposed (Ferrari F, et al., Solitomab, an EpCAM/CD3 bispecific antibody construct (BiTE®), is highly active against primary uterine and ovarian carcinosarcoma cell lines in vitro. J Exp Clin Cancer Res. 2015 34:123). Monoclonal antibodies to EpCAM are known in the art. EpCAM monoclonal ING-1, 3622W94, adecatumumab and edrecolomab are described as tested in human patients (M

nz, M. Side-by-side analysis of five clinically tested anti-EpCAM monoclonal antibodies Cancer Cell International, 10:44-56, 2010). Bispecific antibodies directed against EpCAM and CD3 have also been described, in which hybridomas producing monoclonal antibodies against EpCAM are fused with either of the two hybridomas OKT3 and 9.3 to form two different bispecific antibodies. construction of anti-antibodies (Mφller, SA, Reisfeld, RA, Bispecific-monoclonal-antibody-directed lysis of ovarian carcinoma cells by activated human T lymphocytes. Cancer Immunol. Immunother. 33:210-216, 1991). Other examples of bispecific antibodies to EpCAM are BiUII, (anti-CD3 (rat) x anti-EpCAM (mouse)) (Zeidler, J. Immunol., 1999, 163:1247-1252), scFv CD3/17- 1A-bispecific (Mack, M. A small bispecific antibody composition expressed as a functional single-chain molecule with high tumor cell cytotoxicity. Proc. Natl. Acad. Sci., 1995, 92:7021-7025), and anti- A partially humanized bispecific diabody with CD3 and anti-EpCAM specificity (Helfrich, W. Construction and characterization of a bispecific diabody for retargeting T cells to human carcinomas. Int. J. Cancer, 1998, 76:232-239) includes

Anti-CCR5 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen CCR5. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for CCR5 and another binding domain (eg, having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to CCR5. Monoclonal antibodies against CCR5 are known in the art. Some embodiments of a binding domain that has binding affinity for the marker/antigen CCR5 may include anti-CCR5 VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for the marker/antigen CCR5 may comprise VH and VL regions, wherein each VH and VL region is a paired VL and VH sequence of anti-CCR5 antibody/antibodies. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen CCR5 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for CCR5 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-CD19 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen CD19. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for CD19 and another binding domain (eg, having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to CD19. Monoclonal antibodies to CD19 are known in the art. Illustrative, non-limiting example(s) of CD19 monoclonal antibodies and their VL and VH sequences are set forth in Table 6 . Some embodiments of a binding domain with binding affinity for the marker/antigen CD19 may include the anti-CD19 VL and VH sequence(s) shown in Table 6 . Some embodiments of a binding domain having binding affinity for the marker/antigen CD19 may include VH and VL regions, wherein each VH and VL region is an anti-CD19 antibody/antibody of Table 6 (e.g. , MT103) at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 93% ) 94%, or at least (about) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or the same do. Some embodiments of a binding domain having binding affinity for the marker/antigen CD19 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from the respective VL and VH sequence(s) shown in Table 6 . In some embodiments of the compositions of the present disclosure, the binding domain specific for CD19 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-HER-2 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen HER-2. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for HER-2 and another binding domain (eg, having a specific binding affinity for effector cells) can include The binding domain may include a VL and a VH derived from a monoclonal antibody to HER-2. Monoclonal antibodies to HER-2 are known in the art. Illustrative and non-limiting example(s) of HER-2 monoclonal antibodies and their VL and VH sequences are set forth in Table 6 . Some embodiments of a binding domain with binding affinity for the marker/antigen HER-2 may include the anti-HER-2 VL and VH sequence(s) shown in Table 6 . Some embodiments of a binding domain that has binding affinity for the marker/antigen HER-2 may include VH and VL regions, wherein each VH and VL region is one of the anti-HER-2 antibodies/antibodies of Table 6. at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94% of the paired VL and VH sequence(s); or at least (about) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are the same. Some embodiments of a binding domain having binding affinity for the marker/antigen HER-2 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from each of the VL and VH sequence(s) shown in Table 6 . In some embodiments of the compositions of the present disclosure, the binding domain specific for HER-2 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-HER-3 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen HER-3. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for HER-3 and another binding domain (eg, having a specific binding affinity for effector cells) can include The binding domain may include a VL and a VH derived from a monoclonal antibody to HER-3. Monoclonal antibodies to HER-3 are known in the art. Illustrative, non-limiting example(s) of HER-3 monoclonal antibodies and their VL and VH sequences are set forth in Table 6 . Some embodiments of a binding domain having binding affinity for the marker/antigen HER-3 may include the anti-HER-3 VL and VH sequence(s) shown in Table 6 . Some embodiments of a binding domain that has binding affinity for the marker/antigen HER-3 may include VH and VL regions, wherein each VH and VL region is one of the anti-HER-3 antibodies/antibodies of Table 6. at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94% of the paired VL and VH sequence(s); or at least (about) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are the same. Some embodiments of a binding domain having binding affinity for the marker/antigen HER-3 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from each of the VL and VH sequence(s) shown in Table 6 . In some embodiments of the compositions of the present disclosure, the binding domain specific for HER-3 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-HER-4 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen HER-4. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for HER-4 and another binding domain (eg, having a specific binding affinity for effector cells) can include The binding domain may include a VL and a VH derived from a monoclonal antibody to HER-4. Monoclonal antibodies to HER-4 are known in the art. Illustrative, non-limiting example(s) of HER-4 monoclonal antibodies and their VL and VH sequences are set forth in Table 6 . Some embodiments of a binding domain with binding affinity for the marker/antigen HER-4 may include the anti-HER-4 VL and VH sequence(s) set forth in Table 6 . Some embodiments of a binding domain that has binding affinity for the marker/antigen HER-4 may include VH and VL regions, wherein each VH and VL region is one of the anti-HER-4 antibodies/antibodies of Table 6. at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94% of the paired VL and VH sequence(s); or at least (about) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are the same. Some embodiments of a binding domain having binding affinity for the marker/antigen HER-4 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from each of the VL and VH sequence(s) shown in Table 6 . In some embodiments of the compositions of the present disclosure, the binding domain specific for HER-4 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-EGFR (Epidermal Growth Factor Receptor) Binding Domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen EGFR. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for EGFR and another binding domain (eg, having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to EGFR. Monoclonal antibodies against EGFR are known in the art. Illustrative, non-limiting example(s) of EGFR monoclonal antibodies and their VL and VH sequences are set forth in Table 6 . Some embodiments of a binding domain with binding affinity for the marker/antigen EGFR may include the anti-EGFR VL and VH sequence(s) shown in Table 6 . Some embodiments of a binding domain having binding affinity for the marker/antigen EGFR may include VH and VL regions, wherein each VH and VL region is an anti-EGFR antibody/antibody paired VL of Table 6. and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 94% of the VH sequence(s). ) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen EGFR include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from the respective VL and VH sequence(s) shown in Table 6 . In some embodiments of the compositions of the present disclosure, the binding domain specific for EGFR may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-PSMA binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen PSMA (Prostate Specific Membrane Antigen). Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for PSMA and another binding domain (e.g., having a specific binding affinity for effector cells). can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to PSMA. Monoclonal antibodies to PSMA are known in the art. Illustrative and non-limiting example(s) of PSMA monoclonal antibodies and their VL and VH sequences are set forth in Table 6 . Some embodiments of a binding domain with binding affinity for the marker/antigen PSMA may include the anti-PSMA VL and VH sequence(s) shown in Table 6 . Some embodiments of a binding domain that has binding affinity for the marker/antigen PSMA may include VH and VL regions, wherein each VH and VL region is an anti-PSMA antibody/paired VL of the antibodies of Table 6. and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 94% of the VH sequence(s). ) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen PSMA include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from the respective VL and VH sequence(s) shown in Table 6 . In some embodiments of the compositions of the present disclosure, the binding domain specific for PSMA may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-CEA binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen CEA (Carcinoembryonic Antigen). Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for CEA and another binding domain (e.g., having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to CEA. Monoclonal antibodies to CEA are known in the art. Illustrative and non-limiting example(s) of CEA monoclonal antibodies and their VL and VH sequences are set forth in Table 6 . Some embodiments of a binding domain with binding affinity for the marker/antigen CEA may include the anti-CEA VL and VH sequence(s) shown in Table 6 . Some embodiments of a binding domain having binding affinity for marker/antigen CEA may include VH and VL regions, wherein each VH and VL region is an anti-CEA antibody/paired VL of antibodies of Table 6. and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 94% of the VH sequence(s). ) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for marker/antigen CEA include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from the respective VL and VH sequence(s) shown in Table 6 . In some embodiments of the compositions of the present disclosure, the binding domain specific for CEA may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-MUC1 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen MUC1. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for MUC1 and another binding domain (e.g., having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to MUC1. Monoclonal antibodies to MUC1 are known in the art. Illustrative and non-limiting example(s) of MUC1 monoclonal antibodies and their VL and VH sequences are set forth in Table 6 . Some embodiments of a binding domain with binding affinity for the marker/antigen MUC1 may include the anti-MUC1 VL and VH sequence(s) shown in Table 6 . Some embodiments of a binding domain having binding affinity for the marker/antigen MUC1 may include VH and VL regions, wherein each VH and VL region is a paired VL of the anti-MUC1 antibody/antibodies of Table 6. and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 94% of the VH sequence(s). ) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen MUC1 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from the respective VL and VH sequence(s) shown in Table 6 . In some embodiments of the compositions of the present disclosure, the binding domain specific for MUC1 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-MUC2 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen MUC2. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for MUC2 and another binding domain (e.g., having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to MUC2. Monoclonal antibodies to MUC2 are known in the art. Some embodiments of a binding domain that has binding affinity for the marker/antigen MUC2 may include anti-MUC2 VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for the marker/antigen MUC2 may include VH and VL regions, wherein each VH and VL region is a paired VL and VH sequence of anti-MUC2 antibody/antibodies. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen MUC2 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for MUC2 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-MUC3 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen MUC3. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for MUC3 and another binding domain (e.g., having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to MUC3. Monoclonal antibodies to MUC3 are known in the art. Some embodiments of a binding domain that has binding affinity for the marker/antigen MUC3 may include anti-MUC3 VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for the marker/antigen MUC3 may comprise VH and VL regions, wherein each VH and VL region is a paired VL and VH sequence of anti-MUC3 antibody/antibodies. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen MUC3 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for MUC3 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-MUC4 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen MUC4. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for MUC4 and another binding domain (e.g., having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to MUC4. Monoclonal antibodies to MUC4 are known in the art. Some embodiments of a binding domain that has binding affinity for the marker/antigen MUC4 may include anti-MUC4 VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for the marker/antigen MUC4 may include VH and VL regions, wherein each VH and VL region is a paired VL and VH sequence of an anti-MUC4 antibody/antibodies. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen MUC4 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for MUC4 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-MUC5AC binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen MUC5AC. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for MUC5AC and another binding domain (e.g., having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to MUC5AC. Monoclonal antibodies to MUC5AC are known in the art. Some embodiments of a binding domain that has binding affinity for the marker/antigen MUC5AC may include anti-MUC5AC VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for the marker/antigen MUC5AC may comprise VH and VL regions, wherein each VH and VL region is a paired VL and VH sequence of anti-MUC5AC antibody/antibodies. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen MUC5AC include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for MUC5AC may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-MUC5B binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen MUC5B. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for MUC5B and another binding domain (e.g., having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to MUC5B. Monoclonal antibodies to MUC5B are known in the art. Some embodiments of a binding domain that has binding affinity for the marker/antigen MUC5B may include anti-MUC5B VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for the marker/antigen MUC5B may comprise VH and VL regions, wherein each VH and VL region is a paired VL and VH sequence of an anti-MUC5B antibody/antibodies. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen MUC5B include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for MUC5B may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-MUC7 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen MUC7. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for MUC7 and another binding domain (e.g., having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to MUC7. Monoclonal antibodies to MUC7 are known in the art. Some embodiments of a binding domain that has binding affinity for the marker/antigen MUC7 may include anti-MUC7 VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for the marker/antigen MUC7 may include VH and VL regions, wherein each VH and VL region is a paired VL and VH sequence of anti-MUC7 antibody/antibodies. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen MUC7 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for MUC7 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-βhCG binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen βhCG. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for βhCG and another binding domain (e.g., having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to βhCG. Monoclonal antibodies to βhCG are known in the art. Some embodiments of a binding domain that has binding affinity for the marker/antigen βhCG may include anti-βhCG VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for marker/antigen βhCG may include VH and VL regions, wherein each VH and VL region is an anti-βhCG antibody/paired VL and VH sequences of antibodies. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen βhCG include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for βhCG may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-Lewis-Y binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen Lewis-Y. Some embodiments of the compositions of the present disclosure are a bispecific bioactive assembly comprising a binding domain specific for Lewis-Y and another binding domain (eg, having a specific binding affinity for effector cells) can include The binding domain may include a VL and a VH derived from a monoclonal antibody to Lewis-Y. Monoclonal antibodies to Lewis-Y are known in the art. Illustrative and non-limiting example(s) of Lewis-Y monoclonal antibodies and their VL and VH sequences are set forth in Table 6 . Some embodiments of a binding domain with binding affinity for the marker/antigen Lewis-Y may include the anti-Lewis-Y VL and VH sequence(s) shown in Table 6 . Some embodiments of a binding domain that has binding affinity for the marker/antigen Lewis-Y may include VH and VL regions, wherein each VH and VL region is one of the anti-Lewis-Y antibodies/antibodies of Table 6. at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94% of the paired VL and VH sequence(s); or at least (about) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are the same. Some embodiments of a binding domain having binding affinity for marker/antigen Lewis-Y include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from each of the VL and VH sequence(s) shown in Table 6 . In some embodiments of the compositions of the present disclosure, the binding domain specific for Lewis-Y may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-CD20 binding domain

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen CD20. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for CD20 and another binding domain (e.g., having a specific binding affinity for effector cells). can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to CD20. Monoclonal antibodies to CD20 are known in the art. Illustrative and non-limiting example(s) of CD20 monoclonal antibodies and their VL and VH sequences are set forth in Table 6 . Some embodiments of a binding domain with binding affinity for the marker/antigen CD20 may include the anti-CD20 VL and VH sequence(s) shown in Table 6 . Some embodiments of a binding domain having binding affinity for the marker/antigen CD20 may include VH and VL regions, wherein each VH and VL region is a paired VL of the anti-CD20 antibody/antibodies of Table 6. and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 94% of the VH sequence(s). ) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen CD20 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from the respective VL and VH sequence(s) shown in Table 6 . In some embodiments of the compositions of the present disclosure, the binding domain specific for CD20 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-CD33 binding domain

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen CD33. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for CD33 and another binding domain (e.g., having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to CD33. Monoclonal antibodies to CD33 are known in the art. Illustrative, non-limiting example(s) of CD33 monoclonal antibodies and their VL and VH sequences are set forth in Table 6 . Some embodiments of a binding domain with binding affinity for the marker/antigen CD33 may include the anti-CD33 VL and VH sequence(s) shown in Table 6 . Some embodiments of a binding domain having binding affinity for the marker/antigen CD33 may comprise VH and VL regions, wherein each VH and VL region is a paired VL of anti-CD33 antibody/antibodies of Table 6. and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 94% of the VH sequence(s). ) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen CD33 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from the respective VL and VH sequence(s) shown in Table 6 . In some embodiments of the compositions of the present disclosure, the binding domain specific for CD33 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-CD30 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen CD30. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for CD30 and another binding domain (e.g., having a specific binding affinity for effector cells). can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to CD30. Monoclonal antibodies to CD30 are known in the art. Some embodiments of a binding domain that has binding affinity for the marker/antigen CD30 may include anti-CD30 VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for the marker/antigen CD30 may comprise VH and VL regions, wherein each VH and VL region is a paired VL and VH sequence of anti-CD30 antibody/antibodies. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen CD30 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for CD30 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-ganglioside GD3 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen ganglioside GD3. Some embodiments of the compositions of the present disclosure include a bispecific bioactive binding domain comprising a binding domain specific for ganglioside GD3 and another binding domain (e.g., having a specific binding affinity for effector cells). assembly may be included. The binding domain may include a VL and a VH derived from a monoclonal antibody to the ganglioside GD3. Monoclonal antibodies to the ganglioside GD3 are known in the art. Some embodiments of a binding domain having binding affinity for the marker/antigen ganglioside GD3 may include anti-ganglioside GD3 VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for the marker/antigen ganglioside GD3 may include VH and VL regions, wherein each VH and VL region is a pair of anti-ganglioside GD3 antibodies/antibodies. at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94% of the VL and VH sequence(s) comprising at least (about) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen ganglioside GD3 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. region, where each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for ganglioside GD3 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-9-O-acetyl-GD3 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen 9-O-acetyl-GD3. Some embodiments of the compositions of the present disclosure are bispecific comprising a binding domain specific for 9-O-acetyl-GD3 and another binding domain (eg, having a specific binding affinity for effector cells). It may contain an enemy bioactive assembly. The binding domain may include a VL and a VH derived from a monoclonal antibody to 9-O-acetyl-GD3. Monoclonal antibodies to 9-O-acetyl-GD3 are known in the art. Some embodiments of a binding domain that has binding affinity for marker/antigen 9-O-acetyl-GD3 may include anti-9-O-acetyl-GD3 VL and VH sequence(s). Some embodiments of a binding domain that has binding affinity for the marker/antigen 9-O-acetyl-GD3 may include VH and VL regions, wherein each VH and VL region is anti-9-O-acetyl-GD3. At least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least ( about) 94%, or at least (about) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity; same. Some embodiments of a binding domain having binding affinity for marker/antigen 9-O-acetyl-GD3 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and CDR-H3 regions, where each can be derived from respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for 9-O-acetyl-GD3 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay. there is.

Anti-globo H binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for marker/antigen Globo H. Some embodiments of the compositions of the present disclosure are bispecific bioactive assemblies comprising a binding domain specific for Globo H and another binding domain (e.g., having a specific binding affinity for effector cells) can include The binding domain may include a VL and a VH derived from a monoclonal antibody to Globo H. Monoclonal antibodies to Globo H are known in the art. Some embodiments of a binding domain that has binding affinity for Marker/Antigen Globo H may include anti-Globo H VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for marker/antigen Globo H may include VH and VL regions, wherein each VH and VL region is a pair of anti-globo H antibodies/antibodies. at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least ( about) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for Marker/Antigen Globo H include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each may be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for Globo H may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-fucosyl GM1 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen fucosyl GM1. Some embodiments of the compositions of the present disclosure are a bispecific bioactive assembly comprising a binding domain specific for fucosyl GM1 and another binding domain (eg, having a specific binding affinity for effector cells) can include The binding domain may include a VL and a VH derived from a monoclonal antibody to fucosyl GM1. Monoclonal antibodies to fucosyl GM1 are known in the art. Some embodiments of a binding domain that has binding affinity for the marker/antigen fucosyl GM1 may include anti-fucosyl GM1 VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for the marker/antigen fucosyl GM1 may include VH and VL regions, wherein each VH and VL region is a pair of anti-fucosyl GM1 antibodies/antibodies. at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least ( about) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen fucosyl GM1 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each may be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for fucosyl GM1 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-GD2 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen GD2. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for GD2 and another binding domain (e.g., having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to GD2. Monoclonal antibodies to GD2 are known in the art. Some embodiments of a binding domain with binding affinity for the marker/antigen GD2 may include anti-GD2 VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for the marker/antigen GD2 may include VH and VL regions, wherein each VH and VL region is a paired VL and VH sequence of anti-GD2 antibody/antibodies. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen GD2 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for GD2 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-carbonic anhydrase IX binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen CA IX (carbonic anhydrase IX). Some embodiments of the compositions of the present disclosure provide a bispecific bioactive assembly comprising a binding domain specific for CA IX and another binding domain (eg, having a specific binding affinity for effector cells) can include The binding domain may include a VL and a VH derived from a monoclonal antibody to CA IX. Monoclonal antibodies to CA IX are known in the art. Some embodiments of a binding domain with binding affinity for the marker/antigen CA IX may include anti-CA IX VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for the marker/antigen CA IX may include VH and VL regions, wherein each VH and VL region comprises a paired VL and VL of anti-CA IX antibody/antibodies. VH sequence(s) at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen CA IX include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. may include, wherein each may be derived from respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for CA IX may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-CD44v6 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen CD44v6. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for CD44v6 and another binding domain (eg, having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to CD44v6. Monoclonal antibodies to CD44v6 are known in the art. Some embodiments of a binding domain that has binding affinity for the marker/antigen CD44v6 may include anti-CD44v6 VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for the marker/antigen CD44v6 may comprise VH and VL regions, wherein each VH and VL region is a paired VL and VH sequence of anti-CD44v6 antibody/antibodies. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen CD44v6 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for CD44v6 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-Sonic Hedgehog (Shh) Binding Domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen Shh (Sonic Hedgehog). Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for Shh and another binding domain (e.g., having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to Shh. Monoclonal antibodies to Shh are known in the art. Some embodiments of a binding domain with binding affinity for marker/antigen Shh may include anti-Shh VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for marker/antigen Shh may include VH and VL regions, wherein each VH and VL region is a paired VL and VH sequence of anti-Shh antibody/antibodies. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for marker/antigen Shh include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for Shh may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-Wue-1 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen Wue-1. Some embodiments of the compositions of the present disclosure are a bispecific bioactive assembly comprising a binding domain specific for Wue-1 and another binding domain (eg, having a specific binding affinity for effector cells) can include The binding domain may include a VL and a VH derived from a monoclonal antibody to Wue-1. Monoclonal antibodies to Wue-1 are known in the art. Some embodiments of a binding domain that has binding affinity for the marker/antigen Wue-1 may include anti-Wue-1 VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for the marker/antigen Wue-1 may include VH and VL regions, wherein each VH and VL region comprises a pair of anti-Wue-1 antibodies/antibodies. at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least ( about) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for marker/antigen Wue-1 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each may be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for Wue-1 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-plasma cell antigen 1 (PC-1) binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen PC-1 (plasma cell antigen). Some embodiments of the compositions of the present disclosure include a dual binding domain comprising a binding domain specific for PC-1 (plasma cell antigen) and another binding domain (eg, having a specific binding affinity for effector cells). It may contain specific bioactive assemblies. The binding domain may include a VL and a VH derived from a monoclonal antibody to PC-1 (plasma cell antigen). Monoclonal antibodies to PC-1 (plasma cell antigen) are known in the art. Some embodiments of a binding domain that has binding affinity for the marker/antigen PC-1 (plasma cell antigen) may include anti-PC-1 (plasma cell antigen) VL and VH sequence(s). Some embodiments of a binding domain that has binding affinity for the marker/antigen PC-1 (plasma cell antigen) may include VH and VL regions, wherein each VH and VL region is anti-PC-1 (plasma cell antigen). cellular antigen) at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93% of the paired VL and VH sequence(s) of the antibody/antibodies, or at least (about) 94%, or at least (about) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity. have or are the same Some embodiments of a binding domain having binding affinity for marker/antigen PC-1 (plasma cell antigen) include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region, wherein each may be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for PC-1 (plasma cell antigen) will have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay. can

Anti-melanoma chondroitin sulfate proteoglycan (MCSP) binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen MCSP (melanoma chondroitin sulfate proteoglycan). Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for MCSP and another binding domain (e.g., having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to MCSP. Monoclonal antibodies to MCSP are known in the art. Some embodiments of a binding domain that has binding affinity for the marker/antigen MCSP may include anti-MCSP VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for the marker/antigen MCSP may include VH and VL regions, wherein each VH and VL region is a paired VL and VH sequence of anti-MCSP antibody/antibodies. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for marker/antigen MCSP include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for MCSP may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-CCR8 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen CCR8. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for CCR8 and another binding domain (e.g., having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to CCR8. Monoclonal antibodies against CCR8 are known in the art. Some embodiments of a binding domain that has binding affinity for the marker/antigen CCR8 may include anti-CCR8 VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for marker/antigen CCR8 may include VH and VL regions, wherein each VH and VL region is a paired VL and VH sequence of anti-CCR8 antibody/antibodies. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen CCR8 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for CCR8 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-prostate 6-transmembrane epithelial antigen (STEAP) binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen STEAP. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for STEAP and another binding domain (e.g., having a specific binding affinity for effector cells). can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to STEAP. Monoclonal antibodies to STEAP are known in the art. Some embodiments of a binding domain that has binding affinity for the marker/antigen STEAP may include anti-STEAP VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for the marker/antigen STEAP may include VH and VL regions, wherein each VH and VL region is a paired VL and VH sequence of an anti-STEAP antibody/antibodies. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for marker/antigen STEAP include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for STEAP may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-mesothelin binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen mesothelin. Some embodiments of the compositions of the present disclosure provide a bispecific bioactive assembly comprising a binding domain specific for mesothelin and another binding domain (eg, having a specific binding affinity for effector cells) can include The binding domain may include a VL and a VH derived from a monoclonal antibody to mesothelin. Monoclonal antibodies to mesothelin are known in the art. Illustrative and non-limiting example(s) of mesothelin monoclonal antibodies and their VL and VH sequences are set forth in Table 6 . Some embodiments of a binding domain with binding affinity for the marker/antigen mesothelin may include the anti-mesothelin VL and VH sequence(s) shown in Table 6 . Some embodiments of a binding domain having binding affinity for the marker/antigen mesothelin may comprise VH and VL regions, wherein each VH and VL region comprises a pair of anti-mesothelin antibodies/antibodies of Table 6. at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen mesothelin include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. can include, wherein each can be derived from each of the VL and VH sequence(s) shown in Table 6 . In some embodiments of the compositions of the present disclosure, the binding domain specific for mesothelin may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-A33 antigen binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for marker/antigen A33. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for A33 and another binding domain (e.g., having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to A33. Monoclonal antibodies to A33 are known in the art. Some embodiments of a binding domain that has binding affinity for marker/antigen A33 may include anti-A33 VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for marker/antigen A33 may include VH and VL regions, wherein each VH and VL region is a paired VL and VH sequence of anti-A33 antibody/antibodies. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for marker/antigen A33 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for A33 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-PSCA binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen PSCA. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for PSCA and another binding domain (e.g., having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to PSCA. Monoclonal antibodies to PSCA are known in the art. Some embodiments of a binding domain that has binding affinity for the marker/antigen PSCA may include anti-PSCA VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for the marker/antigen PSCA may include VH and VL regions, wherein each VH and VL region is a paired VL and VH sequence of an anti-PSCA antibody/antibodies. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for marker/antigen PSCA include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for PSCA may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-Ly-6 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen Ly-6. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for Ly-6 and another binding domain (eg, having a specific binding affinity for effector cells) can include The binding domain may include a VL and a VH derived from a monoclonal antibody to Ly-6. Monoclonal antibodies to Ly-6 are known in the art. Some embodiments of a binding domain that has binding affinity for the marker/antigen Ly-6 may include anti-Ly-6 VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for the marker/antigen Ly-6 may include VH and VL regions, wherein each VH and VL region comprises a pair of anti-Ly-6 antibodies/antibodies. at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least ( about) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen Ly-6 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each may be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for Ly-6 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-SAS binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen SAS. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for SAS and another binding domain (e.g., having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to SAS. Monoclonal antibodies to SAS are known in the art. Some embodiments of a binding domain with binding affinity for marker/antigen SAS may include anti-SAS VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for marker/antigen SAS may include VH and VL regions, wherein each VH and VL region is a paired VL and VH sequence of an anti-SAS antibody/antibodies. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for marker/antigen SAS include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for SAS may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-desmoglein 4 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen desmoglein 4. Some embodiments of the compositions of the present disclosure include a bispecific bioactive binding domain comprising a binding domain specific for desmoglein 4 and another binding domain (e.g., having a specific binding affinity for effector cells). assembly may be included. The binding domain may include a VL and a VH derived from a monoclonal antibody to desmoglein 4. Monoclonal antibodies to desmoglein 4 are known in the art. Some embodiments of a binding domain that has binding affinity for the marker/antigen desmoglein 4 may include anti-desmoglein 4 VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for the marker/antigen desmoglein 4 may include VH and VL regions, wherein each VH and VL region is an anti-desmoglein 4 antibody/pair of antibodies. at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94% of the VL and VH sequence(s) comprising at least (about) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen desmoglein 4 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. region, where each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for desmoglein 4 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-fnAChR (fetal acetylcholine receptor) binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen fnAChR (fetal acetylcholine receptor). Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for fnAChR and another binding domain (e.g., having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to fnAChR. Monoclonal antibodies to fnAChR are known in the art. Some embodiments of a binding domain that has binding affinity for the marker/antigen fnAChR may include anti-fnAChR VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for the marker/antigen fnAChR may include VH and VL regions, wherein each VH and VL region is an anti-fnAChR antibody/paired VL and VH sequences of antibodies. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen fnAChR include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for fnAChR may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-CD25 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen CD25. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for CD25 and another binding domain (e.g., having a specific binding affinity for effector cells). can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to CD25. Monoclonal antibodies to CD25 are known in the art. Some embodiments of a binding domain that has binding affinity for the marker/antigen CD25 may include anti-CD25 VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for the marker/antigen CD25 may comprise VH and VL regions, wherein each VH and VL region is a paired VL and VH sequence of anti-CD25 antibody/antibodies. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen CD25 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for CD25 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-cancer antigen 19-9 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for marker/antigenic cancer antigen 19-9. Some embodiments of the compositions of the present disclosure are bispecific organisms comprising a binding domain specific for cancer antigen 19-9 and another binding domain (eg, having a specific binding affinity for effector cells). Active assemblies may be included. The binding domain may include a VL and a VH derived from a monoclonal antibody to cancer antigen 19-9. Monoclonal antibodies against cancer antigen 19-9 are known in the art. Some embodiments of a binding domain that has binding affinity for marker/antigen cancer antigen 19-9 may include anti-cancer antigen 19-9 VL and VH sequence(s). Some embodiments of a binding domain that has binding affinity for marker/antigen cancer antigen 19-9 may include VH and VL regions, wherein each VH and VL region is an anti-cancer antigen 19-9 antibody/antibody. at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94% of the paired VL and VH sequence(s) of , or at least (about) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for marker/antigen cancer antigen 19-9 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-L1 region. H3 regions, where each can be derived from respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for cancer antigen 19-9 (CA 19-9) has a K _d of greater than 10 ⁻⁷ to 10 ⁻¹⁰ M, as determined using an in vitro binding assay. can have a value.

Anti-MISIIR binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen MISIIR (Müller inhibitor type II receptor). Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for MISIIR and another binding domain (e.g., having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to MISIIR. Monoclonal antibodies to MISIIR are known in the art. Some embodiments of a binding domain that has binding affinity for the marker/antigen MISIIR may include anti-MISIIR VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for the marker/antigen MISIIR may include VH and VL regions, wherein each VH and VL region is a paired VL and VH sequence of an anti-MISIIR antibody/antibodies. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for marker/antigen MISIIR include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for MISIIR may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-sTn (sialylated Tn antigen) binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen sTn (sialylated Tn antigen). Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for sTn and another binding domain (e.g., having a specific binding affinity for effector cells). can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to sTn. Monoclonal antibodies to sTn are known in the art. Some embodiments of a binding domain that has binding affinity for marker/antigen sTn may include anti-sTn VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for a marker/antigen sTn may include VH and VL regions, wherein each VH and VL region comprises an anti-sTn antibody/paired VL and VH sequences of antibodies. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for marker/antigen sTn include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for sTn may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-FAP binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen FAP. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for FAP and another binding domain (e.g., having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to FAP. Monoclonal antibodies to FAP are known in the art. Some embodiments of a binding domain that has binding affinity for marker/antigen FAP may include anti-FAP VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for a marker/antigen FAP may comprise VH and VL regions, wherein each VH and VL region is an anti-FAP antibody/antibody paired VL and VH sequences. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for marker/antigen FAP include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for FAP may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-CD248 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen CD248. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for CD248 and another binding domain (e.g., having a specific binding affinity for effector cells). can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to CD248. Monoclonal antibodies to CD248 are known in the art. Some embodiments of a binding domain that has binding affinity for the marker/antigen CD248 may include anti-CD248 VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for the marker/antigen CD248 may include VH and VL regions, wherein each VH and VL region is a paired VL and VH sequence of anti-CD248 antibody/antibodies. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen CD248 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for CD248 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-EGFRvIII binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen EGFRvIII. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for EGFRvIII and another binding domain (eg, having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to EGFRvIII. Monoclonal antibodies to EGFRvIII are known in the art. Some embodiments of a binding domain that has binding affinity for the marker/antigen EGFRvIII may include anti-EGFRvIII VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for the marker/antigen EGFRvIII may comprise VH and VL regions, wherein each VH and VL region is a paired VL and VH sequence of an anti-EGFRvIII antibody/antibodies. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen EGFRvIII include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for EGFRvIII may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-TAL6 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen TAL6. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for TAL6 and another binding domain (eg, having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to TAL6. Monoclonal antibodies to TAL6 are known in the art. Some embodiments of a binding domain that has binding affinity for the marker/antigen TAL6 may include anti-TAL6 VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for the marker/antigen TAL6 may comprise VH and VL regions, wherein each VH and VL region comprises an anti-TAL6 antibody/paired VL and VH sequences of antibodies. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for marker/antigen TAL6 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for TAL6 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-CD63 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen CD63. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for CD63 and another binding domain (eg, having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to CD63. Monoclonal antibodies to CD63 are known in the art. Some embodiments of a binding domain with binding affinity for the marker/antigen CD63 may include anti-CD63 VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for the marker/antigen CD63 may comprise VH and VL regions, wherein each VH and VL region is a paired VL and VH sequence of anti-CD63 antibody/antibodies. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen CD63 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for CD63 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-TAG72 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen TAG72. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for TAG72 and another binding domain (e.g., having a specific binding affinity for effector cells). can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to TAG72. Monoclonal antibodies to TAG72 are known in the art. Illustrative and non-limiting example(s) of TAG72 monoclonal antibodies and their VL and VH sequences are set forth in Table 6 . Some embodiments of a binding domain with binding affinity for the marker/antigen TAG72 may include the anti-TAG72 VL and VH sequence(s) shown in Table 6 . Some embodiments of a binding domain having binding affinity for the marker/antigen TAG72 may include VH and VL regions, wherein each VH and VL region is a paired VL of the anti-TAG72 antibody/antibodies of Table 6. and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 94% of the VH sequence(s). ) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen TAG72 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from the respective VL and VH sequence(s) shown in Table 6 . In some embodiments of the compositions of the present disclosure, the binding domain specific for TAG72 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-TF-Antigen Binding Domain:

In some embodiments of the compositions of the present disclosure, a binding domain may have a specific binding affinity for a marker/antigen TF antigen. Some embodiments of the compositions of the present disclosure provide a bispecific bioactive assembly comprising a binding domain specific for a TF antigen and another binding domain (eg, having a specific binding affinity for effector cells) can include The binding domain may include a VL and a VH derived from a monoclonal antibody to a TF antigen. Monoclonal antibodies directed against the TF antigen are known in the art. Some embodiments of a binding domain that has binding affinity for a marker/antigen TF antigen may include anti-TF antigen VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for a marker/antigen TF antigen may include VH and VL regions, wherein each VH and VL region comprises a paired VL and/or anti-TF antigen antibody/antibodies. VH sequence(s) at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for a Marker/Antigen TF antigen include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. may include, wherein each may be derived from respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for a TF antigen may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-IGF-IR binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen IGF-IR. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for IGF-IR and another binding domain (eg, having a specific binding affinity for effector cells) can include The binding domain may include a VL and a VH derived from a monoclonal antibody to IGF-IR. Monoclonal antibodies to IGF-IR are known in the art. Some embodiments of a binding domain with binding affinity for the marker/antigen IGF-IR may include anti-IGF-IR VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for the marker/antigen IGF-IR can include VH and VL regions, wherein each VH and VL region is a pair of anti-IGF-IR antibodies/antibodies. at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least ( about) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen IGF-IR include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each may be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for IGF-IR may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-Corra Antigen Binding Domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for a marker/antigen cora antigen. Some embodiments of the compositions of the present disclosure provide a bispecific bioactive assembly comprising a binding domain specific for a Cora antigen and another binding domain (eg, having a specific binding affinity for an effector cell) can include The binding domain may include a VL and a VH derived from a monoclonal antibody against the Cora antigen. Monoclonal antibodies against the Cora antigen are known in the art. Some embodiments of a binding domain that has binding affinity for the marker/antigen Cora antigen may include anti-Corra antigen VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for a Marker/Antigen Cora Antigen may comprise VH and VL regions, wherein each VH and VL region is a paired VL and VL region of anti-Corra Antigen antibody/antibodies. VH sequence(s) at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for a marker/antigen chora antigen include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. may include, wherein each may be derived from respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for the Cora antigen may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

anti-CD7 binding domain

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen CD7. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for CD7 and another binding domain (e.g., having a specific binding affinity for effector cells). can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to CD7. Monoclonal antibodies to CD7 are known in the art. Some embodiments of a binding domain with binding affinity for marker/antigen CD7 may include anti-CD7 VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for marker/antigen CD7 may include VH and VL regions, wherein each VH and VL region is a paired VL and VH sequence of anti-CD7 antibody/antibodies. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen CD7 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for CD7 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-CD22 binding domain

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen CD22. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for CD22 and another binding domain (e.g., having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to CD22. Monoclonal antibodies to CD22 are known in the art. Some embodiments of a binding domain that has binding affinity for the marker/antigen CD22 may include anti-CD22 VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for the marker/antigen CD22 may include VH and VL regions, wherein each VH and VL region is a paired VL and VH sequence of anti-CD22 antibody/antibodies. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen CD22 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for CD22 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-CD79a binding domain

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen CD79a. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for CD79a and another binding domain (eg, having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to CD79a. Monoclonal antibodies to CD79a are known in the art. Some embodiments of a binding domain that has binding affinity for the marker/antigen CD79a may include anti-CD79a VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for the marker/antigen CD79a may comprise VH and VL regions, wherein each VH and VL region is a paired VL and VH sequence of anti-CD79a antibody/antibodies. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen CD79a include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for CD79a may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-CD79b binding domain

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen CD79b. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for CD79b and another binding domain (e.g., having a specific binding affinity for effector cells). can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to CD79b. Monoclonal antibodies to CD79b are known in the art. Some embodiments of a binding domain that has binding affinity for the marker/antigen CD79b may include anti-CD79b VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for the marker/antigen CD79b may comprise VH and VL regions, wherein each VH and VL region is a paired VL and VH sequence of anti-CD79b antibody/antibodies. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen CD79b include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for CD79b may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-G250 binding domain

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen G250. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for G250 and another binding domain (e.g., having a specific binding affinity for effector cells). can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to G250. Monoclonal antibodies to G250 are known in the art. Some embodiments of a binding domain with binding affinity for marker/antigen G250 may include anti-G250 VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for marker/antigen G250 may include VH and VL regions, wherein each VH and VL region is a paired VL and VH sequence of anti-G250 antibody/antibodies. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for marker/antigen G250 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for G250 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-MT-MMP binding domain

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen MT-MMP. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for MT-MMP and another binding domain (eg, having a specific binding affinity for effector cells) can include The binding domain may include a VL and a VH derived from a monoclonal antibody to MT-MMP. Monoclonal antibodies to MT-MMP are known in the art. Some embodiments of a binding domain that has binding affinity for the marker/antigen MT-MMP may include anti-MT-MMP VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for the marker/antigen MT-MMP may include VH and VL regions, wherein each VH and VL region comprises a pair of anti-MT-MMP antibodies/antibodies. at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least ( about) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen MT-MMP include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each may be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for MT-MMP may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-F19 antigen binding domain

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for marker/antigen F19. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for F19 and another binding domain (e.g., having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to F19. Monoclonal antibodies to F19 are known in the art. Some embodiments of a binding domain that has binding affinity for marker/antigen F19 may include anti-F19 VL and VH sequence(s). Some embodiments of a binding domain having binding affinity for marker/antigen F19 may include VH and VL regions, wherein each VH and VL region is a paired VL and VH sequence of anti-F19 antibody/antibodies. (s) and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% , or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for marker/antigen F19 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from a respective VL and VH sequence(s). In some embodiments of the compositions of the present disclosure, the binding domain specific for F19 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-EphA2 Receptor Binding Domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen EphA2. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for EphA2 and another binding domain (e.g., having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to EphA2. Monoclonal antibodies to EphA2 are known in the art. Illustrative and non-limiting example(s) of EphA2 monoclonal antibodies and their VL and VH sequences are set forth in Table 6 . Some embodiments of a binding domain with binding affinity for the marker/antigen EphA2 may include the anti-EphA2 VL and VH sequence(s) shown in Table 6 . Some embodiments of a binding domain having binding affinity for the marker/antigen EphA2 may comprise VH and VL regions, wherein each VH and VL region is an anti-EphA2 antibody/paired VL of the antibodies of Table 6. and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 94% of the VH sequence(s). ) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen EphA2 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from the respective VL and VH sequence(s) shown in Table 6 . In some embodiments of the compositions of the present disclosure, the binding domain specific for EphA2 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-alpha 4 integrin binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen alpha 4 integrin. Some embodiments of the compositions of the present disclosure are a bispecific bioactive assembly comprising a binding domain specific for alpha 4 integrin and another binding domain (eg, having a specific binding affinity for effector cells) can include The binding domain may include a VL and a VH derived from a monoclonal antibody to alpha 4 integrin. Monoclonal antibodies to alpha 4 integrin are known in the art. Illustrative and non-limiting example(s) of alpha 4 integrin monoclonal antibodies and their VL and VH sequences are set forth in Table 6 . Some embodiments of a binding domain with binding affinity for marker/antigen alpha 4 integrin may include the anti-alpha 4 integrin VL and VH sequence(s) shown in Table 6 . Some embodiments of a binding domain having binding affinity for marker/antigen alpha 4 integrin may include VH and VL regions, wherein each VH and VL region is a paired VL and VL region of the Natalizumab antibody of Table 6 . VH sequence(s) at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for marker/antigen alpha 4 integrin include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from each of the VL and VH sequence(s) shown in Table 6 . In some embodiments of the compositions of the present disclosure, the binding domain specific for alpha 4 integrin may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-Ang2 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen Ang2 (Angiopoietin-2). Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for Ang2 and another binding domain (e.g., having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to Ang2. Monoclonal antibodies to Ang2 are known in the art. Illustrative and non-limiting example(s) of Ang2 monoclonal antibodies and their VL and VH sequences are set forth in Table 6 . Some embodiments of a binding domain with binding affinity for the marker/antigen Ang2 may include the anti-Ang2 VL and VH sequence(s) shown in Table 6 . Some embodiments of a binding domain having binding affinity for the marker/antigen Ang2 may include VH and VL regions, wherein each VH and VL region is a paired VL and VH of the nesvacumab antibody of Table 6. at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% of the sequence(s) %, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are equal. Some embodiments of a binding domain having binding affinity for the marker/antigen Ang2 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from the respective VL and VH sequence(s) shown in Table 6 . In some embodiments of the compositions of the present disclosure, the binding domain specific for Ang2 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-CEACAM5 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen CEACAM5 (Carcinoembryonic Antigen Associated Cell Adhesion Molecule 5). Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for CEACAM5 and another binding domain (eg, having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to CEACAM5. Monoclonal antibodies to CEACAM5 are known in the art. Illustrative and non-limiting example(s) of CEACAM5 monoclonal antibodies and their VL and VH sequences are set forth in Table 6 . Some embodiments of a binding domain with binding affinity for the marker/antigen CEACAM5 may include the anti-CEACAM5 VL and VH sequence(s) shown in Table 6 . Some embodiments of a binding domain having binding affinity for the marker/antigen CEACAM5 may include VH and VL regions, wherein each VH and VL region is a paired VL and VH of the anti-CEACAM5 antibodies of Table 6. at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% of the sequence(s) %, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are equal. Some embodiments of a binding domain having binding affinity for the marker/antigen CEACAM5 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from the respective VL and VH sequence(s) shown in Table 6 . In some embodiments of the compositions of the present disclosure, the binding domain specific for CEACAM5 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-CD38 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen CD38. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for CD38 and another binding domain (e.g., having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to CD38. Monoclonal antibodies to CD38 are known in the art. Illustrative and non-limiting example(s) of CD38 monoclonal antibodies and their VL and VH sequences are set forth in Table 6 . Some embodiments of a binding domain with binding affinity for the marker/antigen CD38 may include the anti-CD38 VL and VH sequence(s) shown in Table 6 . Some embodiments of a binding domain having binding affinity for the marker/antigen CD38 may comprise VH and VL regions, wherein each VH and VL region is a paired VL of the anti-CD38 antibody/antibodies of Table 6. and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 94% of the VH sequence(s). ) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen CD38 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from the respective VL and VH sequence(s) shown in Table 6 . In some embodiments of the compositions of the present disclosure, the binding domain specific for CD38 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-CD70 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen CD70. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for CD70 and another binding domain (e.g., having a specific binding affinity for effector cells). can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to CD70. Monoclonal antibodies to CD70 are known in the art. Illustrative, non-limiting example(s) of CD70 monoclonal antibodies and their VL and VH sequences are set forth in Table 6 . Some embodiments of a binding domain with binding affinity for the marker/antigen CD70 may include the anti-CD70 VL and VH sequence(s) shown in Table 6 . Some embodiments of a binding domain having binding affinity for the marker/antigen CD70 may include VH and VL regions, wherein each VH and VL region is a paired VL and VH of the anti-CD70 antibodies of Table 6. at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% of the sequence(s) %, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are equal. Some embodiments of a binding domain having binding affinity for the marker/antigen CD70 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from the respective VL and VH sequence(s) shown in Table 6 . In some embodiments of the compositions of the present disclosure, the binding domain specific for CD70 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-cMET (mesenchymal epithelial metastasis factor) binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen cMET. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for cMET and another binding domain (e.g., having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to cMET. Monoclonal antibodies to cMET are known in the art. Illustrative and non-limiting example(s) of cMET monoclonal antibodies and their VL and VH sequences are set forth in Table 6 . Some embodiments of a binding domain with binding affinity for the marker/antigen cMET can include the anti-cMET VL and VH sequence(s) shown in Table 6 . Some embodiments of a binding domain that has binding affinity for the marker/antigen cMET can include VH and VL regions, wherein each VH and VL region is a paired VL and VH of the anti-cMET antibodies of Table 6. at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% of the sequence(s) %, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are equal. Some embodiments of a binding domain having binding affinity for the marker/antigen cMET include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from the respective VL and VH sequence(s) shown in Table 6 . In some embodiments of the compositions of the present disclosure, the binding domain specific for cMET may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-CTLA4 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen CTLA4. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for CTLA4 and another binding domain (e.g., having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to CTLA4. Monoclonal antibodies to CTLA4 are known in the art. Illustrative and non-limiting example(s) of CTLA4 monoclonal antibodies and their VL and VH sequences are set forth in Table 6 . Some embodiments of a binding domain with binding affinity for the marker/antigen CTLA4 may include the anti-CTLA4 VL and VH sequence(s) shown in Table 6 . Some embodiments of a binding domain having binding affinity for the marker/antigen CTLA4 may include VH and VL regions, wherein each VH and VL region is a paired VL and VH of the anti-CTLA4 antibodies of Table 6. at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% of the sequence(s) %, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are equal. Some embodiments of a binding domain having binding affinity for the marker/antigen CTLA4 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from the respective VL and VH sequence(s) shown in Table 6 . In some embodiments of the compositions of the present disclosure, the binding domain specific for CTLA4 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-ENPP3 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen ENPP3 (ectonucleotide pyrophosphatase/phosphodiesterase 3). Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for ENPP3 and another binding domain (e.g., having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to ENPP3. Monoclonal antibodies to ENPP3 are known in the art. Illustrative and non-limiting example(s) of ENPP3 monoclonal antibodies and their VL and VH sequences are set forth in Table 6 . Some embodiments of a binding domain with binding affinity for the marker/antigen ENPP3 may include the anti-ENPP3 VL and VH sequence(s) shown in Table 6 . Some embodiments of a binding domain having binding affinity for the marker/antigen ENPP3 may include VH and VL regions, where each VH and VL region is a paired VL and VH of the H16-7.8 antibody of Table 6. at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% of the sequence(s) %, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are equal. Some embodiments of a binding domain having binding affinity for the marker/antigen ENPP3 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from the respective VL and VH sequence(s) shown in Table 6 . In some embodiments of the compositions of the present disclosure, the binding domain specific for ENPP3 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-FOLR1 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen FOLR1. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for FOLR1 and another binding domain (eg, having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to FOLR1. Monoclonal antibodies to FOLR1 are known in the art. Illustrative and non-limiting example(s) of FOLR1 monoclonal antibodies and their VL and VH sequences are set forth in Table 6 . Some embodiments of a binding domain with binding affinity for the marker/antigen FOLR1 may include the anti-FOLR1 VL and VH sequence(s) shown in Table 6 . Some embodiments of a binding domain having binding affinity for the marker/antigen FOLR1 may include VH and VL regions, wherein each VH and VL region is an anti-FOLR1 antibody/paired VL of the antibodies of Table 6. and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 94% of the VH sequence(s). ) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen FOLR1 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region , wherein each can be derived from the respective VL and VH sequence(s) shown in Table 6 . In some embodiments of the compositions of the present disclosure, the binding domain specific for FOLR1 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-GPC3 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen GPC3 (Glypican 3). Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for GPC3 and another binding domain (e.g., having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to GPC3. Monoclonal antibodies to GPC3 are known in the art. Illustrative and non-limiting example(s) of GPC3 monoclonal antibodies and their VL and VH sequences are set forth in Table 6 . Some embodiments of a binding domain with binding affinity for the marker/antigen GPC3 may include the anti-GPC3 VL and VH sequence(s) shown in Table 6 . Some embodiments of a binding domain having binding affinity for the marker/antigen GPC3 may comprise VH and VL regions, wherein each VH and VL region is a paired VL of the anti-GPC3 antibody/antibodies of Table 6. and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 94% of the VH sequence(s). ) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen GPC3 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from the respective VL and VH sequence(s) shown in Table 6 . In some embodiments of the compositions of the present disclosure, the binding domain specific for GPC3 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-PD-L1 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen PD-L1. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for PD-L1 and another binding domain (eg, having a specific binding affinity for effector cells) can include The binding domain may include a VL and a VH derived from a monoclonal antibody to PD-L1. Monoclonal antibodies to PD-L1 are known in the art. Illustrative and non-limiting example(s) of PD-L1 monoclonal antibodies and their VL and VH sequences are set forth in Table 6 . Some embodiments of a binding domain with binding affinity for the marker/antigen PD-L1 may include the anti-PD-L1 VL and VH sequence(s) shown in Table 6 . Some embodiments of a binding domain that has binding affinity for the marker/antigen PD-L1 can include VH and VL regions, wherein each VH and VL region is one of the anti-PD-L1 antibodies/antibodies of Table 6. at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94% of the paired VL and VH sequence(s); or at least (about) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are the same. Some embodiments of a binding domain having binding affinity for marker/antigen PD-L1 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from each of the VL and VH sequence(s) shown in Table 6 . In some embodiments of the compositions of the present disclosure, the binding domain specific for PD-L1 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-ROR1 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen ROR1. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for ROR1 and another binding domain (eg, having a specific binding affinity for effector cells) can do. The binding domain may include a VL and a VH derived from a monoclonal antibody to ROR1. Monoclonal antibodies to ROR1 are known in the art. Illustrative and non-limiting example(s) of ROR1 monoclonal antibodies and their VL and VH sequences are set forth in Table 6 . Some embodiments of a binding domain with binding affinity for the marker/antigen ROR1 may include the anti-ROR1 VL and VH sequence(s) shown in Table 6 . Some embodiments of a binding domain having binding affinity for the marker/antigen ROR1 may include VH and VL regions, wherein each VH and VL region is a paired VL of the anti-ROR1 antibody/antibodies of Table 6. and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 94% of the VH sequence(s). ) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen ROR1 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from the respective VL and VH sequence(s) shown in Table 6 . In some embodiments of the compositions of the present disclosure, the binding domain specific for ROR1 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-TPBG/5T4 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen TPBG/5T4 (trophoblast glycoprotein). Some embodiments of the compositions of the present disclosure are bispecific bioactive assemblies comprising a binding domain specific for TPBG/5T4 and another binding domain (e.g., having a specific binding affinity for effector cells) can include The binding domain may include VL and VH derived from a monoclonal antibody to TPBG/5T4. Monoclonal antibodies to TPBG/5T4 are known in the art. Illustrative and non-limiting example(s) of TPBG/5T4 monoclonal antibodies and their VL and VH sequences are set forth in Table 6 . Some embodiments of a binding domain with binding affinity for the marker/antigen TPBG/5T4 may include the anti-TPBG/5T4 VL and VH sequence(s) shown in Table 6 . Some embodiments of a binding domain that has binding affinity for the marker/antigen TPBG/5T4 can include VH and VL regions, wherein each VH and VL region is one of the anti-TPBG/5T4 antibodies/antibodies of Table 6. at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94% of the paired VL and VH sequence(s); or at least (about) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are the same. Some embodiments of a binding domain having binding affinity for the marker/antigen TPBG/5T4 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from each of the VL and VH sequence(s) shown in Table 6 . In some embodiments of the compositions of the present disclosure, the binding domain specific for TPBG/5T4 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-TROP-2 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen TROP-2. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for TROP-2 and another binding domain (eg, having a specific binding affinity for effector cells) can include The binding domain may include a VL and a VH derived from a monoclonal antibody to TROP-2. Monoclonal antibodies to TROP-2 are known in the art. Illustrative, non-limiting example(s) of TROP-2 monoclonal antibodies and their VL and VH sequences are set forth in Table 6 . Some embodiments of a binding domain with binding affinity for the marker/antigen TROP-2 may include the anti-TROP-2 VL and VH sequence(s) shown in Table 6 . Some embodiments of a binding domain having binding affinity for the marker/antigen TROP-2 may include VH and VL regions, wherein each VH and VL region is one of the anti-TROP-2 antibodies/antibodies of Table 6. at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94% of the paired VL and VH sequence(s); or at least (about) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are the same. Some embodiments of a binding domain having binding affinity for marker/antigen TROP-2 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from each of the VL and VH sequence(s) shown in Table 6 . In some embodiments of the compositions of the present disclosure, the binding domain specific for TROP-2 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-VEGFR1 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen VEGFR1. Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for VEGFR1 and another binding domain (eg, having a specific binding affinity for effector cells) can do. The binding domain may include VL and VH derived from a monoclonal antibody to VEGFR1. Monoclonal antibodies against VEGFR1 are known in the art. Illustrative and non-limiting example(s) of VEGFR1 monoclonal antibodies and their VL and VH sequences are set forth in Table 6 . Some embodiments of a binding domain with binding affinity for the marker/antigen VEGFR1 may include the anti-VEGFR1 VL and VH sequence(s) shown in Table 6 . Some embodiments of a binding domain having binding affinity for the marker/antigen VEGFR1 may include VH and VL regions, wherein each VH and VL region is a paired VL of the anti-VEGFR1 antibody/antibodies of Table 6. and at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 94% of the VH sequence(s). ) 95%, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are identical. Some embodiments of a binding domain having binding affinity for the marker/antigen VEGFR1 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from the respective VL and VH sequence(s) shown in Table 6 . In some embodiments of the compositions of the present disclosure, the binding domain specific for VEGFR1 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

Anti-VEGFR2 binding domain:

In some embodiments of the compositions of the present disclosure, the binding domain may have a specific binding affinity for the marker/antigen VEGFR2 (vascular endothelial growth factor receptor 2). Some embodiments of the compositions of the present disclosure include a bispecific bioactive assembly comprising a binding domain specific for VEGFR2 and another binding domain (eg, having a specific binding affinity for effector cells) can do. The binding domain may include VL and VH derived from a monoclonal antibody to VEGFR2. Monoclonal antibodies against VEGFR2 are known in the art. Illustrative and non-limiting example(s) of VEGFR2 monoclonal antibodies and their VL and VH sequences are set forth in Table 6 . Some embodiments of a binding domain with binding affinity for the marker/antigen VEGFR2 may include the anti-VEGFR2 VL and VH sequence(s) shown in Table 6 . Some embodiments of a binding domain having binding affinity for the marker/antigen VEGFR2 may include VH and VL regions, wherein each VH and VL region is a paired VL and VH of the anti-VEGFR2 antibodies of Table 6. at least (about) 90%, or at least (about) 91%, or at least (about) 92%, or at least (about) 93%, or at least (about) 94%, or at least (about) 95% of the sequence(s) %, or at least (about) 96%, or at least (about) 97%, or at least (about) 98%, or at least (about) 99% identity, or are equal. Some embodiments of a binding domain having binding affinity for the marker/antigen VEGFR2 include a CDR-L1 region, a CDR-L2 region, a CDR-L3 region, a CDR-H1 region, a CDR-H2 region, and a CDR-H3 region. , wherein each can be derived from the respective VL and VH sequence(s) shown in Table 6 . In some embodiments of the compositions of the present disclosure, the binding domain specific for VEGFR2 may have a K _d value between 10 ⁻⁷ and greater than 10 ⁻¹⁰ M, as determined using an in vitro binding assay.

It is specifically contemplated that a composition of the present disclosure may include any one of the foregoing binding domains or sequence variants thereof, so long as the variant exhibits binding specificity for the described antigen. Sequence variants can be created by substituting amino acids in the VL or VH sequences with different amino acids. In deletion variants, one or more amino acid residues within the VL or VH sequences as described herein are removed. Deletion variants thus include all fragments of the binding domain polypeptide sequence. In substitutional variants, one or more amino acid residues of a VL or VH (or CDR) polypeptide are removed and replaced with alternative residues. Substitutions can be conservative in nature, and conservative substitutions of this type are well known in the art. It is also specifically contemplated that compositions comprising the first and second binding domains disclosed herein may be used in any of the methods disclosed herein.

Exemplary Activatable Therapeutics

In some embodiments of the compositions of the present disclosure, the activatable therapeutic agent is a recombinant polypeptide comprising an amino acid sequence having at least (about) 80% sequence identity to a sequence set forth in Table 7 or a subset thereof. The activatable therapeutic agent is at least (about) 81%, at least (about) 82%, at least (about) 83%, at least (about) 84%, at least (about) 85%, at least about a sequence set forth in Table 7 or a subset thereof. (about) 86%, at least (about) 87%, at least (about) 88%, at least (about) 89%, at least (about) 90%, at least (about) 91%, at least (about) 92%, at least ( About) 93%, at least (about) 94%, at least (about) 95%, at least (about) 96%, at least (about) 97%, at least (about) 98%, or at least (about) 99% sequence identity It may include an amino acid sequence having. An activatable therapeutic agent may comprise an amino acid sequence identical to the sequence set forth in Table 7 or a subset thereof. Compositions of the present disclosure may be composed of those with inserted linker sequence(s) or attached purification tag sequence(s), as long as the variants exhibit substantially similar or identical bioactivity/biological activities and/or activation mechanism(s). As such, it is specifically contemplated that it may include sequence variants of the amino acid sequences set forth in Table 7 or a subset thereof.

Table 7. Amino acid sequences of exemplary recombinant polypeptides

target tissue or cell

In some embodiments of a composition (eg, a therapeutic agent or activatable therapeutic agent described above) or method described herein, the target tissue or cell is cleaved by a mammalian protease at a cleavage sequence (eg, those described in Table A ). A reporter polypeptide (eg, described in this target tissue or cell section herein), which may be contained therein or on it, or associated with the reporter polypeptide in proximity thereto. A reporter polypeptide can be a polypeptide set forth in the “Report Protein” column of Table A (or any subset thereof). In some embodiments, the reporter polypeptide is a coagulation factor, complement component, tubulin, immunoglobulin, apolipoprotein, serum amyloid, insulin, growth factor, fibrinogen, PDZ domain protein, LIM domain protein, c-reactive protein, serum albumin, versican, collagen, elastin, keratin, kininogen-1, alpha-2-antiplasmin, clustererin, biglycan, alpha-1-antitrypsin, transthyretin, alpha-1-antichymotrypsin, Glucagon, hepcidin, thymosin beta-4, haptoglobin, hemoglobin subunit alpha, vesicle-associated protein 2, alpha-2-HS-glycoprotein, chromogranin-A, vitronectin, hemopexin, epididymal secreting sperm binding protein, secretogranin-2, angiotensinogen, transgelin-2, pancreatic prohormone, neurosecretory protein VGF, ceruloplasmin, PDZ and LIM domain protein 1, multimerin-1, inter-alpha- Trypsin inhibitor heavy chain H2, N-acetylmuramoyl-L-alanine amidase, histone H1.4, adhesion G-protein coupled receptor G6, mannan binding lectin serine protease 2, prothrombin, 1 protein deleted in malignant brain tumors (deleted in malignant brain tumors 1 protein), desmoglein-3, calcintenin-1, alpha-2-macroglobulin, myosin-9, sodium/potassium transport ATPase subunit gamma, oncoprotein-derived transcript 3 protein, serglycine, histidine rich glycoprotein, inter-alpha-trypsin inhibitor heavy chain H5, integrin alpha-IIb, membrane associated progesterone receptor component 1, histone H1.2, rho GDP-dissociation inhibitor 2, zinc-alpha-2-glycoprotein, Talin-1, Secretogranin-1, Neutrophil Defensin 3, Cytochrome P450 2E1, Gastric Inhibitory Polypeptide, Transcription Initiation Factor TFIID Subunit 1, Integral Membrane Protein 2B, Pigmented Epithelial Derived Factor, Voltage-dependent Type N Calcium Channel Subunit alpha-1B, ras GTPase-activating protein nGAP, type I cytoskeleton 17, sulfhydryl oxidase 1, homeobox protein Hox-B2, transcription factor SOX-10, E3 ubiquitin-protein ligase SIAH2, decorin, cysteine secreted protein acidic and rich in cysteine (SPARC), laminin gamma 1 chain, vimentin and nidogen-1 (NID1). In some embodiments, the reporter polypeptide is collagen, elastin, keratin, coagulation factor, complement component, tubulin, immunoglobulin, apolipoprotein, serum amyloid, insulin, growth factor, fibrinogen, PDZ domain protein, LIM domain protein, c- reactive proteins and serum albumin. Collagen is type I collagen, type II collagen, type III collagen, type IV collagen, type V collagen, type VI collagen, type VII collagen, type VIII collagen, type IX collagen, type X collagen, type XI collagen, type XII collagen, Type XIII Collagen, Type XIV Collagen, Type XV Collagen, Type XVI Collagen, Type XVII Collagen, Type XVIII Collagen, Type XIX Collagen, Type XX Collagen, Type XXI Collagen, Type XXII Collagen, Type XXIII Collagen, Type XXIV Collagen, Type XXV comprising the alpha chain(s) (e.g., alpha-1, alpha-2, alpha-3, or combinations thereof) of collagen, type XXVI collagen, type XXVII collagen, type XXVIII collagen, type XXIX collagen, or combinations thereof can do. The coagulation factor may be selected from coagulation factor IX, coagulation factor XII, coagulation factor XIII A chain. Complement components include C1 (eg, complement C1r subcomponent-like proteins, complement C1r subcomponent, but not limited to), C3, C4 (eg, complement C4-A, complement C4-B, but not limited to) and C5. Tubulin may be selected from tubulin alpha chain (eg, tubulin alpha-4A chain) and tubulin beta chain. Immunoglobulins are immunoglobulin lambda variable 3-21, immunoglobulin lambda variable 3-25, immunoglobulin lambda variable 1-51, immunoglobulin lambda variable 1-36, immunoglobulin kappa variable 3-20, immunoglobulin kappa variable 2-30. , possible non-functional immunoglobulin kappa variable 2D-24, immunoglobulin lambda constant 3, immunoglobulin kappa variable 2-28, immunoglobulin kappa variable 3-11, immunoglobulin kappa variable 1-39, immunoglobulin lambda variable 6-57, immunoglobulin kappa variable 3-15, immunoglobulin lambda variable 2-18, immunoglobulin heavy chain variable 3-15, immunoglobulin lambda variable 2-11, immunoglobulin lambda variable 3-27 and immunoglobulin kappa variable 4-1. can The apolipoprotein can be selected from apolipoprotein AI, apolipoprotein AI isoform 1, apolipoprotein C-III, apolipoprotein CI, apolipoprotein A-II and apolipoprotein L1. The serum amyloid protein can be selected from serum amyloid A-1 protein and serum amyloid A-2 protein. The growth factor may be selected from insulin-like growth factor II, potential transforming growth factor beta binding protein 2 and potential transforming growth factor beta binding protein 4. Fibrinogen may be selected from fibrinogen alpha chain, fibrinogen beta chain and fibrinogen gamma chain. LIM domain proteins can be straight. In some embodiments, the reporter polypeptide is versican, type II collagen alpha-1 chain, kininogen-1, complement C4-A, complement C4-B, complement C3, alpha-2-antiplasmin, clustererin , biglycan, elastin, fibrinogen alpha chain, alpha-1-antitrypsin, fibrinogen beta chain, type III collagen alpha-1 chain, serum amyloid A-1 protein, transthyretin, apolipoprotein AI, apolipoprotein AI iso Type 1, alpha-1-antichymotrypsin, glucagon, hepcidin, serum amyloid A-2 protein, thymosin beta-4, haptoglobin, hemoglobin subunit alpha, vesicle-associated protein 2, alpha-2-HS-sugar Protein, chromogranin-A, vitronectin, hemopexin, epididymal secreted sperm binding protein, direct skin, apolipoprotein C-III, secretogranin-2, angiotensinogen, c-reactive protein, serum albumin, Transgelin-2, pancreatic prohormone, neurosecretory protein VGF, ceruloplasmin, PDZ and LIM domain protein 1, tubulin alpha-4A chain, multimerin-1, inter-alpha-trypsin inhibitor heavy chain H2, apolipoprotein CI, fibrinogen gamma chain, N-acetylmuramoyl-L-alanine amidase, immunoglobulin lambda variable 3-21, histone H1.4, attachment G-protein coupled receptor G6, immunoglobulin lambda variable 3-25, immunoglobulin lambda Variable 1-51, immunoglobulin lambda variable 1-36, mannan-binding lectin serine protease 2, immunoglobulin kappa variable 3-20, immunoglobulin kappa variable 2-30, insulin-like growth factor II, apolipoprotein A-II, potential nonfunctional immunoglobulin kappa variable 2D-24, prothrombin, coagulation factor IX, apolipoprotein L1, protein 1 deleted in malignant brain tumor, desmoglein-3, calcintenin-1, immunoglobulin lambda constant 3, complement C5 , alpha-2-macroglobulin, myosin-9, sodium/potassium transport ATPase subunit gamma, immunoglobulin kappa variable 2-28, oncoprotein-derived transcript 3 protein, serglycine, coagulation factor XII, coagulation factor XIII A chain, insulin, histidine rich glycoprotein, immunoglobulin kappa variable 3-11, immunoglobulin kappa variable 1-39, collagen alpha-1(I) chain, inter-alpha-trypsin inhibitor heavy chain H5, potential transforming growth factor beta binding protein 2, Integrin alpha-IIb, membrane associated progesterone receptor component 1, immunoglobulin lambda variable 6-57, immunoglobulin kappa variable 3-15, complement C1r subcomponent-like protein, histone H1.2, Rho GDP-dissociation inhibitor 2, potential transforming growth Factor beta binding protein 4, collagen alpha-1 (XVIII) chain, immunoglobulin lambda variable 2-18, zinc-alpha-2-glycoprotein, talin-1, secretogranin-1, neutrophil defensin 3, cytochrome P450 2E1, Gastric Inhibitory Polypeptide, Immunoglobulin Heavy Chain Variable 3-15, Immunoglobulin Lambda Variable 2-11, Transcription Initiation Factor TFIID Subunit 1, Collagen Alpha-1 (VII) Chain, Integral Membrane Protein 2B, Pigmented Epithelial Derived Factor, Voltage dependent type N calcium channel subunit alpha-1B, immunoglobulin lambda variable 3-27, ras GTPase-activating protein nGAP, keratin, type I cytoskeleton 17, tubulin beta chain, sulfhydryl oxidase 1, immunoglobulin kappa variable 4-1, complement C1r subcomponent, homeobox protein Hox-B2, transcription factor SOX-10, E3 ubiquitin-protein ligase SIAH2, decorin, SPARC, type I collagen alpha-1 chain, type IV collagen alpha-1 chain, laminin gamma 1 chain, vimentin, collagen type III, collagen type IV alpha-3 chain, collagen type VII alpha-1 chain, collagen type VI alpha-1 chain, collagen type V alpha-1 chain, nidogen-1 and type VI collagen alpha-3 chains. In some embodiments, the reporter polypeptide is a cleavage sequence set forth in column II or III of Table A (or a subset thereof) and/or a group set forth in Tables 1(a)-1(j) (or any subset thereof). can include Reporter polypeptides can include the sequences set forth in column IV of Table A (or a subset thereof). Reporter polypeptides can include the sequences set forth in column V of Table A (or a subset thereof). Reporter polypeptides can include the sequences set forth in column VI of Table A (or a subset thereof). A reporter polypeptide can include a peptide biomarker (or peptide biomarker sequence) that can be identified from a biological sample of a subject (eg, those set forth in Table A ). Peptide biomarkers can include the sequences set forth in column IV of Table A (or a subset thereof). Peptide biomarkers can include the sequences set forth in column V of Table A (or a subset thereof). Peptide biomarkers can include the sequences set forth in column VI of Table A (or a subset thereof). In some embodiments, the reporter polypeptide is selected from the group set forth in column I of Table A (or a subset thereof). In some embodiments, the cleavage sequence of the reporter polypeptide does not include a methionine residue immediately N-terminal to a cleavable bond (contained therein) if methionine is the first residue N-terminal to the reporter polypeptide.

Table A. Exemplary Cleavage Sequences and Biomarker Sequences in Exemplary Reporter Polypeptides

* (Putative) cleavable bonds of each cleavage sequence listed in Table A , cleavage sequence 1 and cleavage sequence 2 (if present) of each reporter polypeptide are indicated by hyphens (-).

“N/A” indicates that the amino acid sequence of the corresponding cleavage sequence is not or cannot be specified where applicable.

In some embodiments of a composition (e.g., a therapeutic agent or activatable therapeutic agent described above) or a method described herein, (cleavage of the releasing segment (RS) or the first releasing segment (RS1), or the second releasing segment (RS2)) For) mammalian proteases can be serine proteases, cysteine proteases, aspartate proteases, threonine proteases or metalloproteinases. Mammalian proteases (for cleavage of the release segment (RS), or the first release segment (RS1), or the second release segment (RS2)) include disintegrin and metalloproteinase domain containing protein 10 (ADAM10), dis Integrin and metalloproteinase domain-containing protein 12 (ADAM12), disintegrin and metalloproteinase domain-containing protein 15 (ADAM15), disintegrin and metalloproteinase domain-containing protein 17 (ADAM17), disintegrin and Metalloproteinase domain containing protein 9 (ADAM9), disintegrin with thrombospondin motif 5 and metalloproteinase (ADAMTS5), cathepsin B, cathepsin D, cathepsin E, cathepsin K, cathepsin L, cathepsin S, fibroblast activation protein alpha, hepsin, kallikrein-2, kallikrein-4, kallikrein-3, prostate specific antigen (PSA), kallikrein-13, legumain, matrix metallopep tidase 1 (MMP-1), matrix metallopeptidase 10 (MMP-10), matrix metallopeptidase 11 (MMP-11), matrix metallopeptidase 12 (MMP-12), matrix metal Lopeptidase 13 (MMP-13), Matrix Metallopeptidase 14 (MMP-14), Matrix Metallopeptidase 16 (MMP-16), Matrix Metallopeptidase 2 (MMP-2), Matrix Metallopeptidase 3 (MMP-3), Matrix Metallopeptidase 7 (MMP-7), Matrix Metallopeptidase 8 (MMP-8), Matrix Metallopeptidase 9 (MMP-9) ), matrix metallopeptidase 4 (MMP-4), matrix metallopeptidase 5 (MMP-5), matrix metallopeptidase 6 (MMP-6), matrix metallopeptidase 15 (MMP -15), neutrophil elastase, protease activated receptor 2 (PAR2), plasmin, prostacin, PSMA-FOLH1, membrane type serine protease 1 (MT-SP1), matriptase and u-plasminogen. can be selected from the group. Mammalian proteases (for cleavage of the release segment (RS), or the first release segment (RS1), or the second release segment (RS2)) are matrix metallopeptidase 1 (MMP1), matrix metallopeptidase 2 (MMP2), matrix metallopeptidase 7 (MMP7), matrix metallopeptidase 9 (MMP9), matrix metallopeptidase 11 (MMP11), matrix metallopeptidase 14 (MMP14), uro kinase-type plasminogen activator (uPA), legumain and matriptase. A mammalian protease may be preferentially expressed or activated in a target tissue or cell.

In some embodiments of a composition (e.g., a therapeutic agent or activatable therapeutic agent described above) or a method described herein, the target tissue or cell is a mammalian protease (proximate to the target tissue or cell compared to a non-target tissue or cell of the subject). eg, as described herein) may be characterized by an increased amount or activity. The target tissue or cell is at least (about) 10%, at least (about) 20%, at least (about) 30%, at least (about) 40%, at least ( about) 50%, at least (about) 60%, at least (about) 70%, at least (about) 80%, at least (about) 90%, at least (about) 100% or at least (about) 200% greater amount may be characterized by the presence of a mammalian protease. The target tissue or cell is at least (about) 10%, at least (about) 20%, at least (about) 30%, at least (about) 40%, at least ( about) 50%, at least (about) 60%, at least (about) 70%, at least (about) 80%, at least (about) 90%, at least (about) 100% or at least (about) 200% higher The activity of the protease can be characterized. The target tissue or cell can produce or colocalize with a mammalian protease (eg, described herein). The target tissue or cell may be a tumor.

In some embodiments, a composition of the present disclosure (eg, an activatable therapeutic agent) is formulated not only to localize the target tissue protease, but also to the same protease in healthy tissue that is not intended to be targeted to provide a broad therapeutic window, as well as unhealthy tissue proteases. It is designed to take into account the greater presence of the ligand in the target tissue. "Therapeutic window" refers to the largest difference between the minimum effective dose and the maximum tolerated dose for a given therapeutic composition. To help achieve a broad therapeutic window, the binding affinity of the intact composition for one or both of the ligands is reduced compared to the composition cleaved by a mammalian protease to release the biologically active moiety from the masking effect of the masking moiety. To do so, the binding domain of the composition is masked by the proximity of a masking moiety (eg, XTEN).

Nucleic acids, expression vectors, host cells

In some embodiments, provided herein is an isolated nucleic acid comprising: (a) a polynucleotide encoding a recombinant polypeptide described herein; or (b) the reverse complement of the polynucleotide of (a).

In some embodiments, an expression vector is provided herein, the expression vector comprising a polynucleotide sequence as described herein and a recombination control sequence operably linked to the polynucleotide sequence.

In some embodiments, provided herein is an isolated host cell, wherein the isolated host cell comprises an expression vector as described herein. The isolated host cell may be prokaryotic. The isolated host cell may be E. coli. An isolated host cell can be a mammalian cell(s).

pharmaceutical composition

In some embodiments, provided herein is a pharmaceutical composition comprising a therapeutic agent (eg, described above or elsewhere herein) and one or more pharmaceutically suitable excipients. The pharmaceutical composition may be formulated for oral, intradermal, subcutaneous, intravenous, intraarterial, intraperitoneal, intraperitoneal, intrathecal or intramuscular administration. A pharmaceutical composition may be in liquid or frozen form. The pharmaceutical composition may be presented as a pre-filled syringe for single injection. Pharmaceutical compositions may be formulated as lyophilized powders that are reconstituted prior to administration.

kit

In some embodiments, a kit is provided herein, the kit comprising a pharmaceutical composition as described herein (or a therapeutic agent described herein), a container, and a label or package insert on or associated with the container.

method

Methods to Assess Potential for Response to Treatment(s)

In some embodiments, provided herein is a method for assessing the likelihood that a subject will respond to a therapeutic agent that can be activated by a mammalian protease expressed in the subject, the method comprising:

(a) Determining the presence or amount of in a biological sample from a subject

(i) at least 4, at least 5, at least 6, at least 7, at least 8, at least 9 or at least 10 contiguous amino acid residues represented in the sequences set forth in column V of Table A (or a subset thereof); Polypeptides, including; or

(ii) comprises at least 4, at least 5, at least 6, at least 7, at least 8, at least 9 or at least 10 contiguous amino acids shown in the sequence set forth in column IV (or a subset thereof) of Table A; a polypeptide that; or

(iii) contains at least 4, at least 5, at least 6, at least 7, at least 8, at least 9 or at least 10 contiguous amino acids shown in the sequence set forth in column VI of Table A (or a subset thereof); a polypeptide that; and

(b) designating the subject as likely to respond to the therapeutic agent if the polypeptide of (i), (ii) or (iii) is present and/or the amount exceeds a threshold value.

In some embodiments of methods for assessing the likelihood of a subject responding to a therapeutic agent, the therapeutic agent may include a peptide substrate susceptible to cleavage by a mammalian protease (eg, at a bond susceptible to cleavage). Peptide substrates can be susceptible to cleavage by mammalian proteases at cleavable bonds. The polypeptide of (i), (ii), or (iii) may comprise (e.g., at least 4, at least 5, at least 6, at least 7 at least 8, at least 9, at least 10, at least 11, at least 12, at least 13, at least 14 or at least 15 contiguous amino acid residues). of the peptide substrate (e.g., at least 4, at least 5, at least 6, at least 7, at least 8, at least 9, at least 10, at least 11, at least 12, at least 13, at least 14 or portions containing at least 15 contiguous amino acid residues) may be immediately N-terminal or directly C-terminal of the cleavable bond. The polypeptide of (i) comprises at least 4, at least 5, at least 6, at least 7, at least 8, at least 9 or at least 10 contiguous sequences shown in the sequence set forth in column V of Table A (or a subset thereof). It may contain amino acid residues. The polypeptide of (i) may comprise the sequence set forth in column V of Table A (or a subset thereof). The polypeptide of (ii) comprises at least 4, at least 5, at least 6, at least 7, at least 8, at least 9 or at least 10 contiguous sequences shown in the sequences set forth in column IV (or a subset thereof) of Table A. May contain amino acids. The polypeptide of (ii) may comprise the sequence set forth in column IV of Table A (or a subset thereof). The polypeptide of (iii) comprises at least 4, at least 5, at least 6, at least 7, at least 8, at least 9 or at least 10 contiguous sequences shown in the sequence set forth in column VI (or a subset thereof) of Table A. May contain amino acids. The polypeptide of (iii) may comprise the sequence set forth in column VI of Table A (or a subset thereof). In some embodiments of the method for assessing likelihood, (a) includes determining the presence or amount of any two of (i) to (iii). In some embodiments of the method for assessing likelihood, (a) comprises determining the presence or amount of all three of (i)-(iii). Additionally or alternatively, the methods described herein in the section entitled "Methods for Assessing Potential for Response to Therapeutic Agent(s)" as being likely to respond to an activatable therapeutic agent (eg, those described herein). A subject designated by a can, when administering an activatable therapeutic agent (eg, as described herein) to the subject, eg, by a mammalian protease(s), in tissue(s) or cell(s) (eg, herein). It can be a subject that has an expression profile of the biomarker(s) such that the activatable therapeutic agent is not cleaved at or near it (as described in the "Target Tissue or Cell" section of <RTI ID=0.0>()</RTI> so that it is likely to activate the therapeutic agent. In some embodiments of the method for assessing likelihood, the threshold may be zero or a nominal threshold. The peptide substrate may be any of the peptide substrates described in the Release Segment section above or elsewhere herein. The activatable therapeutic agent can be any therapeutic agent (or any activatable therapeutic agent, or any non-natural activatable therapeutic agent) described in the Therapeutic Agents section above or anywhere else herein. The mammalian protease can be any mammalian protease described in the Target Tissue or Cell section above or elsewhere herein. The target tissue or cell can be any of those described in the Target Tissues or Cells section above or elsewhere herein. The target tissue or cell may be a tumor.

In some embodiments of the method for assessing viability, the biological sample may be selected from serum, plasma, blood, spinal fluid, semen, and saliva. A biological sample may include a serum or plasma sample. A biological sample may include a serum sample. A biological sample may include a plasma sample. A biological sample may include a blood sample. A biological sample may include a spinal fluid sample. A biological sample may include a semen sample. A biological sample may include a saliva sample.

In some embodiments of the method for assessing likelihood, a subject is compared to a corresponding non-target tissue or cell of the subject, compared to a target tissue or cell (e.g., described in the target tissue or cell section of the stomach or any other herein). described elsewhere) may be suffering from or suspected of suffering from a disease or condition characterized by increased expression or activity of a mammalian protease. The subject can be selected from mouse, rat, monkey and human. The subject may be a human. In some embodiments, the disease or condition may be cancer or an inflammatory or autoimmune disease. In some embodiments, the disease or condition may be cancer. Cancers include carcinoma, Hodgkin's lymphoma and non-Hodgkin's lymphoma, diffuse large B-cell lymphoma, follicular lymphoma, mantle cell lymphoma, blastoma, breast cancer, ER/PR+ breast cancer, Her2+ breast cancer, triple negative breast cancer, colorectal cancer, and malignant ascites. Colon cancer, mucinous tumor, prostate cancer, head and neck cancer, skin cancer, melanoma, genitourinary cancer, ovarian cancer, ovarian cancer with malignant ascites, peritoneal carcinomatosis, uterine serous carcinoma, endometrial cancer, cervical cancer, colorectal cancer , uterine cancer, peritoneal mesothelioma, renal cancer, Wilms tumor, lung cancer, small cell lung cancer, non-small cell lung cancer, gastric cancer, stomach cancer, small intestine cancer, liver cancer, hepatocarcinoma, hepatoblastoma, liposarcoma, pancreatic cancer, gallbladder cancer, cholangiocarcinoma , esophageal cancer, salivary gland carcinoma, thyroid cancer, epithelial cancer, male germ cell tumor, adenocarcinoma, sarcoma, and B-cell derived chronic lymphocytic leukemia. In some embodiments, the disease or condition may be an inflammatory or autoimmune disease. Inflammatory or autoimmune diseases include but are not limited to ankylosing spondylitis (AS), arthritis (eg, rheumatoid arthritis (RA), juvenile idiopathic arthritis (JIA), osteoarthritis (OA), psoriatic arthritis (PsA), gout, chronic arthritis) not known), Chagas disease, chronic obstructive pulmonary disease (COPD), dermatomyositis, type 1 diabetes, endometriosis, Goodpasture syndrome, Graves disease, Guillain-Barré syndrome (GBS), Hashimoto disease, purulent scab, Kawasaki disease, IgA nephropathy, idiopathic thrombocytopenic purpura, inflammatory bowel disease (IBD) (eg, Crohn's disease (CD), clonal disease, ulcerative colitis, collagen colitis, lymphocytic colitis, ischemic colitis, empty colitis, Behçet's syndrome, infectious colitis, indeterminate colitis, interstitial cystitis, but not limited to), lupus (eg, systemic lupus erythematosus, discoid lupus, subacute cutaneous lupus erythematosus, cutaneous lupus erythematosus (eg, alumni) lupus erythematosus), drug-induced lupus, neonatal lupus, lupus nephritis (but not limited to), mixed connective tissue disease, focal scleroderma, multiple sclerosis (MS), severe muscle weakness, narcolepsy, neuromuscular angina, pemphigus vulgaris ; Wegener's granulomatosis, immune response associated with transplant rejection (eg, but not limited to, kidney transplant rejection, lung transplant rejection, liver transplant rejection), psoriasis, Wiskott-Aldrich syndrome, autoimmune lymphoproliferative syndrome, myasthenia gravis, Inflammatory chronic rhinosinusitis, colitis, chronic dyspepsia, Barrett's esophagus, inflammatory gastritis, autoimmune nephritis, autoimmune hepatitis, autoimmune carditis, autoimmune encephalitis, autoimmune mediated blood disorders, asthma, atopic dermatitis, atopy, It may be selected from the group consisting of allergy, allergic rhinitis, scleroderma, bronchitis, and pericarditis, and the inflammatory disease is Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis, inflammatory lung disease, inflammatory skin disease, atherosclerosis, myocardial infarction, Stroke, gram-positive shock, gram-negative shock, sepsis, septic shock, hemorrhagic shock, anaphylactic shock, and systemic inflammatory response syndrome. Additionally or alternatively, the methods described herein in the section entitled "Methods for Assessing Potential for Response to Therapeutic Agent(s)" as being likely to respond to an activatable therapeutic agent (eg, those described herein). A subject designated by a can, when administering an activatable therapeutic agent (eg, as described herein) to the subject, eg, by a mammalian protease(s), in tissue(s) or cell(s) (eg, herein). It can be a subject that has an expression profile of the biomarker(s) such that the activatable therapeutic agent is not cleaved at or near it (as described in the "Target Tissue or Cell" section of <RTI ID=0.0>()</RTI> so that it is likely to activate the therapeutic agent. In some embodiments, the method for assessing likelihood may further include transmitting the designation details to a health care provider and/or subject. In some embodiments, the method for evaluating potential may further comprise (b) thereafter contacting the therapeutic agent with a mammalian protease. In some embodiments, the method for assessing likelihood may further include, after (b), administering to the subject an effective amount of a therapeutic agent based on the specifications in step (b). In some embodiments of the method for assessing likelihood, (a) may include detecting the polypeptide of (i), (ii) or (iii) in an immunoassay. The immunoassay may use an antibody that specifically binds to the polypeptide of (i), (ii) or (iii) or an epitope thereof. In some embodiments of the method for assessing likelihood, (a) is performed using mass spectrometry (MS) (including but not limited to LC-MS, LC-MS/MS, etc.) to (i), (ii) or detecting the polypeptide of (iii).

Methods of making the therapeutic agent(s)

In some embodiments, provided herein is a method of making an activatable therapeutic comprising:

(a) culturing a host cell comprising a nucleic acid construct encoding the recombinant polypeptide under conditions sufficient to allow expression of the recombinant polypeptide in the host cell, wherein the recombinant polypeptide comprises a biologically active polypeptide (BP), a release segment (RS) and a masking moiety (MM),

RS comprises a peptide substrate susceptible to cleavage by a mammalian protease at its cleavable linkage, the peptide substrate comprising a sequence set forth in column II or column III of Table A (or a subset thereof) and/or Tables 1(a)- comprising an amino acid sequence having at least 80% sequence identity to the group set forth in 1(j) ; and

The recombinant polypeptide has a structural arrangement from the N-terminus to the C-terminus of BP-RS-MM or MM-RS-BP; and

(b) recovering the activatable therapeutic comprising the recombinant polypeptide.

In some embodiments of the method of making an activatable therapeutic agent, the releasing segment (RS) can be the first releasing segment (RS1), the peptide substrate can be the first peptide substrate, and the cleavable bond is first cleaved. may be readily conjugated, the masking moiety (MM) may be a first masking moiety (MM1), and the recombinant polypeptide may further comprise a second releasing segment (RS2) and a second masking moiety (MM2) there is, here

RS2 comprises a second peptide substrate susceptible to cleavage by a mammalian protease at its cleavable linkage, the second peptide substrate comprising a sequence set forth in column II or column III of Table A (or a subset thereof) and/or Table 1 (a) can comprise an amino acid sequence having at least 80% sequence identity to the groups set forth in -1(j) ;

The recombinant polypeptide is C- from the N-terminus of MM1-RS1-BP-RS2-MM2, MM1-RS2-BP-RS1-MM2, MM2-RS1-BP-RS2-MM1, or MM2-RS2-BP-RS1-MM1. It may have a structural arrangement up to the end.

In some embodiments of the methods of making an activatable therapeutic agent, the masking moiety (MM) is an extended recombinant polypeptide (XTEN) (eg, described in the Masking Moieties section above or elsewhere herein) can include In some embodiments of the method of making an activatable therapeutic agent, where the activatable therapeutic agent comprises a first masking moiety (MM1) and a second masking moiety (MM2), one of MM1 and MM2 comprises a first extended recombination polypeptide (XTEN1) (eg, as described in the Masking Moiety section above or elsewhere herein). The other of MM1 and MM2 may include a second extended recombinant polypeptide (XTEN2) (eg, described in the Masking Moiety section above or elsewhere herein).

In some embodiments of the method of making an activatable therapeutic agent, the recombinant polypeptide can be any described herein. The masking moiety (MM), when linked to the recombinant polypeptide, may interfere with the interaction of the biologically active peptide (BP) with the target tissue or cell, resulting in the recombinant polypeptide being incompatible with the target tissue or cell when in an uncleaved state. The dissociation constant (K _d ) of the target cell marker carried by the recombinant polypeptide and the BP of the recombinant polypeptide may be greater compared to the dissociation constant (K _d ) of the corresponding biologically active peptide released from the recombinant polypeptide. The first masking moiety (MM1) and the second masking moiety (MM2), when both are linked in a recombinant polypeptide ( each independently, individually or collectively ), bind to a biologically active peptide (BP) for a target tissue or cell. can interfere with the interaction, as a result of which the dissociation constant (K _d ) of the BP of the recombinant polypeptide and the target cell marker carried by the target tissue or cell when the recombinant polypeptide is in an uncleaved state is reduced in the first release segment ( RS1) and the second release segment (RS2) when one or both are cleaved compared to the dissociation constant (K _d ) of the corresponding biologically active peptide. The dissociation constant (Kd) can be determined in an in vitro assay under equimolar concentrations. In vitro assays include cell membrane integrity assay, mixed cell culture assay, cell-based competitive binding assay, FACS-based propidium iodide assay, trypan blue influx assay, photometric enzyme release assay, radiometric 51Cr release assay, fluorescence assay europium release assay, CalceinAM release assay, photometric MTT assay, XTT assay, WST-1 assay, Alamar blue assay, radiometric assay 3H-Thd incorporation assay, clonogenic assay to measure cell division activity, fluorescence to measure mitochondrial transmembrane gradients a rhodamine 123 assay, a FACS-based apoptosis assay monitored by phosphatidylserine exposure, an ELISA-based TUNEL test assay, a sandwich ELISA, a caspase activity assay, a cell-based LDH release assay, a reporter gene activity assay, and a cell morphology assay; or may be selected from any combination thereof.

Methods of treating a subject with the therapeutic agent(s)

In some embodiments, provided herein is a method of treating a subject with an activatable therapeutic agent, the method comprising:

(a) identifying a subject as likely to respond to an activatable therapeutic based on identification of a peptide biomarker in a biological sample from the subject, wherein the activatable therapeutic is resistant to cleavage by a mammalian protease at a cleavable bond. comprising a fragile peptide substrate; and

(b) administering to the subject an activatable therapeutic agent based on the identification of the subject in (a);

The peptide biomarker herein comprises a portion identical to at least four contiguous amino acid residues of a peptide substrate that is N-terminus or C-terminus of a scissile bond.

In some embodiments described in the immediately preceding paragraph, the peptide substrate may be any peptide substrate described in the Release Segment section above or elsewhere herein. The activatable therapeutic agent can be any therapeutic agent (or any activatable therapeutic agent, or any non-natural activatable therapeutic agent) described in the Therapeutic Agents section above or anywhere else herein. The mammalian protease can be any mammalian protease described in the Target Tissue or Cell section above or elsewhere herein. The peptide biomarker can be any peptide biomarker described in the target tissue or cell section above (eg, as set forth in Table A ) or as described elsewhere herein. Possibility of response may be determined by the methods described in the Methods for Evaluating Potential for Response to Therapeutic Agent(s) section above or described elsewhere herein. At least 5, at least 6, at least 7, at least 8, at least 9, at least 10 of the peptide substrate, wherein the moiety containing at least 4 consecutive amino acid residues is N-terminus or C-terminus of the scissile bond , at least 11, at least 12, at least 13, at least 14 or at least 15 contiguous amino acid residues. at least 4 (e.g., at least 5, at least 6, at least 7, at least 8, at least 9, at least 10, at least 11, at least 12, at least 13, at least 14 of the peptide substrates) or at least 15) contiguous amino acid residues may be immediately N-terminal or immediately C-terminal of the cleavable bond. Additionally or alternatively, the methods described herein in the section entitled "Methods for Assessing Potential for Response to Therapeutic Agent(s)" as being likely to respond to an activatable therapeutic agent (eg, those described herein). A subject designated by a can, when administering an activatable therapeutic agent (eg, as described herein) to the subject, eg, by a mammalian protease(s), in tissue(s) or cell(s) (eg, herein). It can be a subject that has an expression profile of the biomarker(s) such that the activatable therapeutic agent is not cleaved at or near it (as described in the "Target Tissue or Cell" section of <RTI ID=0.0>()</RTI> so that it is likely to activate the therapeutic agent. In some embodiments, a peptide biomarker can be derived from a reporter polypeptide (eg, as described herein). In some embodiments, a peptide biomarker may have an amino acid sequence identical to that of a reporter polypeptide. Reporter polypeptides can include the sequences set forth in columns II-VI of Table A (or a subset thereof). In some embodiments, the peptide substrate comprises an amino acid sequence with up to 3, up to 2, or up to 1 amino acid substitution(s) relative to a sequence set forth in column II or column III of Table A (or a subset thereof). can do. In some embodiments, none of the amino acid substitutions can be at a position corresponding to an amino acid residue immediately adjacent to the corresponding cleavable bond, as shown in Table A. In some embodiments, the peptide substrate may comprise an amino acid sequence set forth in column II or column III of Table A (or a subset thereof). In some embodiments, the peptide substrate can include an amino acid sequence with up to 3, up to 2, or up to 1 amino acid substitution(s) relative to the sequence set forth in Table 1(j) . In some embodiments, none of the amino acid substitutions can be at a position corresponding to an amino acid residue immediately adjacent to the corresponding scissile bond shown in Table 1(j) . In some embodiments, the peptide substrate can include an amino acid sequence set forth in Table 1(j) .

In some embodiments, provided herein is a method of treating a subject in need of a therapeutic agent capable of being activated by a mammalian protease expressed in the subject, the method comprising:

Administering an effective amount of a therapeutic agent to a subject, wherein the subject has been shown to express in a biological sample from the subject:

(i) at least 4, at least 5, at least 6, at least 7, at least 8, at least 9 or at least 10 contiguous amino acid residues indicated in the sequences set forth in column V of Table A (or a subset thereof); Polypeptides, including; or

(ii) comprises at least 4, at least 5, at least 6, at least 7, at least 8, at least 9 or at least 10 contiguous amino acids shown in the sequence set forth in column IV (or a subset thereof) of Table A; a polypeptide that; or

(iii) comprises at least 4, at least 5, at least 6, at least 7, at least 8, at least 9 or at least 10 contiguous amino acids shown in the sequence set forth in column VI of Table A (or a subset thereof); a polypeptide that; or

(iv) The expression level of polypeptide (i), (ii) or (iii) exceeds a threshold value.

In some embodiments described in the immediately preceding paragraph, the threshold may be zero or a nominal threshold. The peptide substrate may be any of the peptide substrates described in the Release Segment section above or elsewhere herein. The activatable therapeutic agent can be any therapeutic agent (or any activatable therapeutic agent, or any non-natural activatable therapeutic agent) described in the Therapeutic Agents section above or anywhere else herein. The mammalian protease can be any mammalian protease described in the Target Tissue or Cell section above or elsewhere herein. Possibility of response may be determined by the methods described in the Methods for Evaluating Potential for Response to Therapeutic Agent(s) section above or described elsewhere herein. The polypeptide of (i) comprises at least 4, at least 5, at least 6, at least 7, at least 8, at least 9 or at least 10 contiguous sequences shown in the sequence set forth in column V of Table A (or a subset thereof). It may contain amino acid residues. The polypeptide of (i) may comprise the sequence set forth in column V of Table A (or a subset thereof). The polypeptide of (ii) comprises at least 4, at least 5, at least 6, at least 7, at least 8, at least 9 or at least 10 contiguous sequences shown in the sequences set forth in column IV (or a subset thereof) of Table A. May contain amino acids. The polypeptide of (ii) may comprise the sequence set forth in column IV of Table A (or a subset thereof). The polypeptide of (iii) comprises at least 4, at least 5, at least 6, at least 7, at least 8, at least 9 or at least 10 contiguous sequences shown in the sequence set forth in column VI (or a subset thereof) of Table A. May contain amino acids. The polypeptide of (iii) may comprise the sequence set forth in column VI of Table A (or a subset thereof). The therapeutic agent may include a peptide substrate that is susceptible to cleavage by mammalian proteases (eg, at a bond susceptible to cleavage). The peptide substrate may be susceptible to cleavage by mammalian proteases at the cleavable linkage, and the polypeptide of (i), (ii), or (iii) is the peptide substrate N-terminus or C-terminus of the cleavable linkage. of (e.g., at least 4, at least 5, at least 6, at least 7, at least 8, at least 9, at least 10, at least 11, at least 12, at least 13, at least 14 or containing at least 15 contiguous amino acid residues). of the peptide substrate (e.g., at least 4, at least 5, at least 6, at least 7, at least 8, at least 9, at least 10, at least 11, at least 12, at least 13, at least 14 or portions containing at least 15 contiguous amino acid residues) may be immediately N-terminal or directly C-terminal of the cleavable bond. In some embodiments, the subject has been shown to express any two of (i) to (iii) in a biological sample. In some embodiments, the subject has been shown to express all three of (i) to (iii) in a biological sample.

In some embodiments of the methods described in the Methods of Treating a Subject with this therapeutic agent(s) section herein, the biological sample can be selected from serum, plasma, blood, spinal fluid, semen, and saliva. A biological sample may include a serum or plasma sample. A biological sample may include a serum sample. A biological sample may include a plasma sample. A biological sample may include a blood sample. A biological sample may include a spinal fluid sample. A biological sample may include a semen sample. A biological sample may include a saliva sample.

In some embodiments of the methods described in the Methods of Treating a Subject with this therapeutic agent(s) section herein, the subject is treated with a target tissue or cell (e.g., a target tissue of the stomach) compared to a corresponding non-target tissue or cell of the subject. or may be suffering from, or suspected of suffering from, a disease or condition characterized by increased expression or activity of a mammalian protease proximal to the cell section or described elsewhere herein). The subject can be selected from mouse, rat, monkey and human. The subject may be a human. A subject can be determined to have a potential response to a therapeutic agent or pharmaceutical composition. The probability of reaction may be greater than 50%. Possibility of response can be determined by methods described herein (eg, as described in the Methods for Evaluating Potential for Response to Therapeutic Agent(s) section above). In some embodiments, the disease or condition may be cancer or an inflammatory or autoimmune disease. In some embodiments, the disease or condition may be cancer. Cancers include carcinoma, Hodgkin's lymphoma and non-Hodgkin's lymphoma, diffuse large B-cell lymphoma, follicular lymphoma, mantle cell lymphoma, blastoma, breast cancer, ER/PR+ breast cancer, Her2+ breast cancer, triple negative breast cancer, colorectal cancer, and malignant ascites. Colon cancer, mucinous tumor, prostate cancer, head and neck cancer, skin cancer, melanoma, genitourinary cancer, ovarian cancer, ovarian cancer with malignant ascites, peritoneal carcinomatosis, uterine serous carcinoma, endometrial cancer, cervical cancer, colorectal cancer , uterine cancer, peritoneal mesothelioma, renal cancer, Wilms tumor, lung cancer, small cell lung cancer, non-small cell lung cancer, gastric cancer, stomach cancer, small intestine cancer, liver cancer, hepatocarcinoma, hepatoblastoma, liposarcoma, pancreatic cancer, gallbladder cancer, cholangiocarcinoma , esophageal cancer, salivary gland carcinoma, thyroid cancer, epithelial cancer, male germ cell tumor, adenocarcinoma, sarcoma, and B-cell derived chronic lymphocytic leukemia. In some embodiments, the disease or condition may be an inflammatory or autoimmune disease. Inflammatory or autoimmune diseases include but are not limited to ankylosing spondylitis (AS), arthritis (eg, rheumatoid arthritis (RA), juvenile idiopathic arthritis (JIA), osteoarthritis (OA), psoriatic arthritis (PsA), gout, chronic arthritis) not known), Chagas disease, chronic obstructive pulmonary disease (COPD), dermatomyositis, type 1 diabetes, endometriosis, Goodpasture syndrome, Graves disease, Guillain-Barré syndrome (GBS), Hashimoto disease, purulent scab, Kawasaki disease, IgA nephropathy, idiopathic thrombocytopenic purpura, inflammatory bowel disease (IBD) (eg, Crohn's disease (CD), clonal disease, ulcerative colitis, collagen colitis, lymphocytic colitis, ischemic colitis, empty colitis, Behçet's syndrome, infectious colitis, indeterminate colitis, interstitial cystitis, but not limited to), lupus (eg, systemic lupus erythematosus, discoid lupus, subacute cutaneous lupus erythematosus, cutaneous lupus erythematosus (eg, alumni) lupus erythematosus), drug-induced lupus, neonatal lupus, lupus nephritis (but not limited to), mixed connective tissue disease, focal scleroderma, multiple sclerosis (MS), severe muscle weakness, narcolepsy, neuromuscular angina, pemphigus vulgaris ; Wegener's granulomatosis, immune response associated with transplant rejection (eg, but not limited to, kidney transplant rejection, lung transplant rejection, liver transplant rejection), psoriasis, Wiskott-Aldrich syndrome, autoimmune lymphoproliferative syndrome, myasthenia gravis, Inflammatory chronic rhinosinusitis, colitis, chronic dyspepsia, Barrett's esophagus, inflammatory gastritis, autoimmune nephritis, autoimmune hepatitis, autoimmune carditis, autoimmune encephalitis, autoimmune mediated blood disorders, asthma, atopic dermatitis, atopy, It may be selected from the group consisting of allergy, allergic rhinitis, scleroderma, bronchitis, and pericarditis, and the inflammatory disease is Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis, inflammatory lung disease, inflammatory skin disease, atherosclerosis, myocardial infarction, Stroke, gram-positive shock, gram-negative shock, sepsis, septic shock, hemorrhagic shock, anaphylactic shock, and systemic inflammatory response syndrome. Additionally or alternatively, the methods described herein in the section entitled "Methods for Assessing Potential for Response to Therapeutic Agent(s)" as being likely to respond to an activatable therapeutic agent (eg, those described herein). A subject designated by a can, when administering an activatable therapeutic agent (eg, as described herein) to the subject, eg, by a mammalian protease(s), in tissue(s) or cell(s) (eg, herein). It can be a subject that has an expression profile of the biomarker(s) such that the activatable therapeutic agent is not cleaved at or near it (as described in the "Target Tissue or Cell" section of <RTI ID=0.0>()</RTI> so that it is likely to activate the therapeutic agent.

Methods and use of the therapeutic agent(s)

In some embodiments, provided herein is a method of treating a disease or condition in a subject, comprising administering to a subject in need thereof one or more therapeutically effective doses of a therapeutic agent (eg, described herein) or a pharmaceutical composition ( eg, as described herein). The subject can be selected from mouse, rat, monkey and human. The subject may be a human. A subject can be determined to have a potential response to a therapeutic agent or pharmaceutical composition. The probability of reaction may be greater than 50%. Possibility of response can be determined by methods described herein (eg, as described in the Methods for Evaluating Potential for Response to Therapeutic Agent(s) section above). In some embodiments, the disease or condition may be cancer or an inflammatory or autoimmune disease. In some embodiments, the disease or condition may be cancer. Cancers include carcinoma, Hodgkin's lymphoma and non-Hodgkin's lymphoma, diffuse large B-cell lymphoma, follicular lymphoma, mantle cell lymphoma, blastoma, breast cancer, ER/PR+ breast cancer, Her2+ breast cancer, triple negative breast cancer, colorectal cancer, and malignant ascites. Colon cancer, mucinous tumor, prostate cancer, head and neck cancer, skin cancer, melanoma, genitourinary cancer, ovarian cancer, ovarian cancer with malignant ascites, peritoneal carcinomatosis, uterine serous carcinoma, endometrial cancer, cervical cancer, colorectal cancer , uterine cancer, peritoneal mesothelioma, renal cancer, Wilms tumor, lung cancer, small cell lung cancer, non-small cell lung cancer, gastric cancer, stomach cancer, small intestine cancer, liver cancer, hepatocarcinoma, hepatoblastoma, liposarcoma, pancreatic cancer, gallbladder cancer, cholangiocarcinoma , esophageal cancer, salivary gland carcinoma, thyroid cancer, epithelial cancer, male germ cell tumor, adenocarcinoma, sarcoma, and B-cell derived chronic lymphocytic leukemia. In some embodiments, the disease or condition may be an inflammatory or autoimmune disease. Inflammatory or autoimmune diseases include but are not limited to ankylosing spondylitis (AS), arthritis (eg, rheumatoid arthritis (RA), juvenile idiopathic arthritis (JIA), osteoarthritis (OA), psoriatic arthritis (PsA), gout, chronic arthritis) not known), Chagas disease, chronic obstructive pulmonary disease (COPD), dermatomyositis, type 1 diabetes, endometriosis, Goodpasture syndrome, Graves disease, Guillain-Barré syndrome (GBS), Hashimoto disease, purulent scab, Kawasaki disease, IgA nephropathy, idiopathic thrombocytopenic purpura, inflammatory bowel disease (IBD) (eg, Crohn's disease (CD), clonal disease, ulcerative colitis, collagen colitis, lymphocytic colitis, ischemic colitis, empty colitis, Behçet's syndrome, infectious colitis, indeterminate colitis, interstitial cystitis, but not limited to), lupus (eg, systemic lupus erythematosus, discoid lupus, subacute cutaneous lupus erythematosus, cutaneous lupus erythematosus (eg, alumni) lupus erythematosus), drug-induced lupus, neonatal lupus, lupus nephritis (but not limited to), mixed connective tissue disease, focal scleroderma, multiple sclerosis (MS), severe muscle weakness, narcolepsy, neuromuscular angina, pemphigus vulgaris ; Wegener's granulomatosis, immune response associated with transplant rejection (eg, but not limited to, kidney transplant rejection, lung transplant rejection, liver transplant rejection), psoriasis, Wiskott-Aldrich syndrome, autoimmune lymphoproliferative syndrome, myasthenia gravis, Inflammatory chronic rhinosinusitis, colitis, chronic dyspepsia, Barrett's esophagus, inflammatory gastritis, autoimmune nephritis, autoimmune hepatitis, autoimmune carditis, autoimmune encephalitis, autoimmune mediated blood disorders, asthma, atopic dermatitis, atopy, It may be selected from the group consisting of allergy, allergic rhinitis, scleroderma, bronchitis, and pericarditis, and the inflammatory disease is Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis, inflammatory lung disease, inflammatory skin disease, atherosclerosis, myocardial infarction, Stroke, gram-positive shock, gram-negative shock, sepsis, septic shock, hemorrhagic shock, anaphylactic shock, and systemic inflammatory response syndrome. Additionally or alternatively, the methods described herein in the section entitled “Methods for Evaluating Potential for Response to Therapeutic Agent(s)” as being likely to respond to an activatable therapeutic agent (eg, those described herein). A subject designated by may, when administering an activatable therapeutic agent (eg, as described herein) to the subject, eg, by a mammalian protease(s), in tissue(s) or cell(s) (eg, herein). It can be a subject that has an expression profile of the biomarker(s) such that the activatable therapeutic agent is not cleaved at or near it (as described in the "Target Tissue or Cell" section of <RTI ID=0.0>(s)</RTI> so that there is a high probability of activating the therapeutic agent.

In some embodiments, provided herein is the use of a therapeutic agent (eg, described herein) or pharmaceutical composition (eg, described herein) in the manufacture of a medicament for the treatment of a disease or condition in a subject. The subject can be selected from mouse, rat, monkey and human. The subject may be a human. A subject can be determined to have a potential response to a therapeutic agent or pharmaceutical composition. The probability of reaction may be greater than 50%. Possibility of response can be determined by methods described herein (eg, as described in the Methods for Evaluating Potential for Response to Therapeutic Agent(s) section above). In some embodiments, the disease or condition may be cancer or an inflammatory or autoimmune disease. In some embodiments, the disease or condition may be cancer. Cancers include carcinoma, Hodgkin's lymphoma and non-Hodgkin's lymphoma, diffuse large B-cell lymphoma, follicular lymphoma, mantle cell lymphoma, blastoma, breast cancer, ER/PR+ breast cancer, Her2+ breast cancer, triple negative breast cancer, colorectal cancer, and malignant ascites. Colon cancer, mucinous tumor, prostate cancer, head and neck cancer, skin cancer, melanoma, genitourinary cancer, ovarian cancer, ovarian cancer with malignant ascites, peritoneal carcinomatosis, uterine serous carcinoma, endometrial cancer, cervical cancer, colorectal cancer , uterine cancer, peritoneal mesothelioma, renal cancer, Wilms tumor, lung cancer, small cell lung cancer, non-small cell lung cancer, gastric cancer, stomach cancer, small intestine cancer, liver cancer, hepatocarcinoma, hepatoblastoma, liposarcoma, pancreatic cancer, gallbladder cancer, cholangiocarcinoma , esophageal cancer, salivary gland carcinoma, thyroid cancer, epithelial cancer, male germ cell tumor, adenocarcinoma, sarcoma, and B-cell derived chronic lymphocytic leukemia. In some embodiments, the disease or condition may be an inflammatory or autoimmune disease. Inflammatory or autoimmune diseases include but are not limited to ankylosing spondylitis (AS), arthritis (eg, rheumatoid arthritis (RA), juvenile idiopathic arthritis (JIA), osteoarthritis (OA), psoriatic arthritis (PsA), gout, chronic arthritis) not known), Chagas disease, chronic obstructive pulmonary disease (COPD), dermatomyositis, type 1 diabetes, endometriosis, Goodpasture syndrome, Graves disease, Guillain-Barré syndrome (GBS), Hashimoto disease, purulent scab, Kawasaki disease, IgA nephropathy, idiopathic thrombocytopenic purpura, inflammatory bowel disease (IBD) (eg, Crohn's disease (CD), clonal disease, ulcerative colitis, collagen colitis, lymphocytic colitis, ischemic colitis, empty colitis, Behçet's syndrome, infectious colitis, indeterminate colitis, interstitial cystitis, but not limited to), lupus (eg, systemic lupus erythematosus, discoid lupus, subacute cutaneous lupus erythematosus, cutaneous lupus erythematosus (eg, alumni) lupus erythematosus), drug-induced lupus, neonatal lupus, lupus nephritis (but not limited to), mixed connective tissue disease, focal scleroderma, multiple sclerosis (MS), severe muscle weakness, narcolepsy, neuromuscular angina, pemphigus vulgaris ; Wegener's granulomatosis, immune response associated with transplant rejection (eg, but not limited to, kidney transplant rejection, lung transplant rejection, liver transplant rejection), psoriasis, Wiskott-Aldrich syndrome, autoimmune lymphoproliferative syndrome, myasthenia gravis, Inflammatory chronic rhinosinusitis, colitis, chronic dyspepsia, Barrett's esophagus, inflammatory gastritis, autoimmune nephritis, autoimmune hepatitis, autoimmune carditis, autoimmune encephalitis, autoimmune mediated blood disorders, asthma, atopic dermatitis, atopy, It may be selected from the group consisting of allergy, allergic rhinitis, scleroderma, bronchitis, and pericarditis, and the inflammatory disease is Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis, inflammatory lung disease, inflammatory skin disease, atherosclerosis, myocardial infarction, Stroke, gram-positive shock, gram-negative shock, sepsis, septic shock, hemorrhagic shock, anaphylactic shock, and systemic inflammatory response syndrome. Additionally or alternatively, the methods described herein in the section entitled "Methods for Assessing Potential for Response to Therapeutic Agent(s)" as being likely to respond to an activatable therapeutic agent (eg, those described herein). A subject designated by a can, when administering an activatable therapeutic agent (eg, as described herein) to the subject, eg, by a mammalian protease(s), in tissue(s) or cell(s) (eg, herein). It can be a subject that has an expression profile of the biomarker(s) such that the activatable therapeutic agent is not cleaved at or near it (as described in the "Target Tissue or Cell" section of <RTI ID=0.0>()</RTI> so that it is likely to activate the therapeutic agent.

Example

Example 1. Recombinant Production of XTENylated Fusion Polypeptides Containing Exemplary Peptide Substrates

This example illustrates the recombinant construction, production and purification of XTENylated fusion polypeptides containing exemplary peptide substrates using the methods disclosed herein.

Expression: An XTENized fusion polypeptide comprising the amino acid sequence of SEQ ID NO: 20 or 22 containing two elastin-based peptide substrates of the sequence GPGG-VAAA (SEQ ID NO: 1283) (shown in #527 of column II of Table A ) The encoding construct is expressed in the native E. coli strain AmE098 and distributed to the periplasm via an N-terminal secretory leader sequence (MKKNIAFLLASMFVFSIATNAYA-) (SEQ ID NO: 3129) that is cleaved during translocation. Fermentation cultures are grown in animal component free complex medium at 37°C, and this temperature is switched to 26°C prior to phosphate depletion. During harvest, the whole fermentation broth is centrifuged to pellet the cells. At harvest, total volume and wet cell weight (WCW; ratio of pellet to supernatant) are recorded, and pelleted cells are collected and frozen at -80°C.

Recovery: The frozen cell pellet is resuspended in lysis buffer (17.7 mM Citric Acid, 22.3 mM Na ₂ HPO ₄ , 75 mM NaCl, 2 mM EDTA, pH 4.0) targeting 30% wet cell weight. The resuspension is equilibrated at pH 4 and then homogenized through 2 passes at 800±50 bar, while the output temperature is monitored and maintained at 15±5° C. Confirm that the pH of the homogenate is within the specified range (pH 4.0 ± 0.2).

Clarification: Homogenates are subjected to low temperature (10±5° C.), acidic (pH 4.0±0.2) flocculation overnight (15-20 hours) to reduce endotoxins and host cell impurities. To remove the insoluble fraction, the aggregated homogenate is centrifuged at 2-8°C at 16,900 RCF for 40 minutes and the supernatant is left as is. The supernatant is diluted approximately 3-fold with Milli-Q water (MQ) and then adjusted to 7±1 mS/cm with 5 M NaCl. The supernatant is adjusted with 0.1% (m/m) diatomaceous earth to remove nucleic acids, lipids and endotoxins and to act as a filter aid. To keep the filter aid suspended, the supernatant is mixed through an impeller and allowed to equilibrate for 30 minutes. A filter train consisting of a depth filter and a 0.22 µm filter is assembled and then flushed with MQ. The supernatant is pumped through the filter train, adjusting the flow to maintain a pressure drop of 25±5 psig. To adjust the complex buffer system (based on the ratio of citric acid to Na ₂ HPO ₄ ) to the desired range for capture chromatography, the filtrate was adjusted with 500 mM of Na ₂ HPO ₄ so that the final ratio of Na ₂ HPO ₄ to citric acid was 9.33: 1, and confirm that the pH of the buffered filtrate is within the specified range (pH 7.0±0.2).

refine

AEX Capture: Electronegative C-terminal XTEN domains are captured using anion exchange (AEX) chromatography to separate dimers, aggregates and large truncations from monomeric products and to remove endotoxins and nucleic acids. AEX1 stationary phase (GE Q Sepharose FF), AEX1 mobile phase A (12.2 mM Na ₂ HPO ₄ , 7.8 mM Na ₂ HPO ₄ , 40 mM NaCl) and AEX1 mobile phase B (12.2 mM Na ₂ HPO ₄ , 7.8 mM Na ₂ HPO ₄ , 500 mM NaCl) is used herein. Equilibrate the column with AEX1 mobile phase A. Based on the total protein concentration determined by the bicinchoninic acid (BCA) assay, the filtrate was loaded onto a column targeting 28±4 g/L-resin, followed by AEX1 mobile phase A, then stepwise to 30% B. wash with Bound material is eluted with a gradient of 30% B to 60% B over 20 CV. When A220 > 100 mAU (local) above baseline, fractions are collected in 1 CV aliquots. Elution fractions are analyzed based on SDS-PAGE and SE-HPLC and pooled.

IMAC intermediate purification: To ensure the integrity of the C-terminus, immobilized metal affinity chromatography (IMAC) is used to capture the C-terminal polyhistidine tag (His(6)). IMAC stationary phase (GE IMAC Sepharose FF), IMAC mobile phase A (18.3 mM Na ₂ HPO ₄ , 1.7 mM Na ₂ HPO ₄ , 500 mM NaCl, 1 mM imidazole) and IMAC mobile phase B (18.3 mM Na 2 HPO ₄ , 1.7 mM Na ₂ HPO 4 ) mM Na ₂ HPO ₄ , 500 mM NaCl, 500 mM imidazole) are used herein. The column is charged with zinc solution and equilibrated with IMAC mobile phase A. The AEX1 pool was adjusted to pH 7.8±0.1, 50±5 mS/cm (with 5 M NaCl) and 1 mM imidazole, loaded onto an IMAC column with 2 g/L-resin as the target, and absorbance at 280 nm. Track with IMAC mobile phase A until (A280) returns to the (local) baseline. The bound material is eluted stepwise to 25% IMAC mobile phase B. When A280 > 10 mAU (local) above baseline, eluate collection is initiated and directed into a container pre-spiked with enough EDTA to make 2 CVs up to 2 mM EDTA, and terminated once 2 CVs have been collected. The eluate is analyzed by SDS-PAGE.

Protein-L intermediate purification: To ensure the integrity of the N-terminus, Protein-L is used to capture the kappa domain located close to the N-terminus of the fusion polypeptide (specifically, the aEpCAM scFv). Protein-L stationary phase (GE Capto L), Protein-L mobile phase A (16.0 mM citric acid, 20.0 mM Na ₂ HPO ₄ , pH 4.0±0.1), Protein-L mobile phase B (29.0 mM citric acid, 7.0 mM Na ₂ HPO ₄ , pH 2.60±0.02) and Protein-L mobile phase C (3.5 mM citric acid, 32.5 mM Na ₂ HPO ₄ , 250 mM NaCl, pH 7.0±0.1) are used herein. Equilibrate the column with Protein-L mobile phase C. The IMAC eluate was adjusted to pH 7.0±0.1 and 30±3 mS/cm (using 5 M NaCl and MQ), loaded with 2 g/L-resin onto a target Protein-L column, and absorbance at 280 nm. Track with protein-L mobile phase C until (A280) returns to the (local) baseline. The column is washed with Protein-L mobile phase A and a low pH elution is performed using Protein-L mobile phases A and B. The bound material is eluted at approximately pH 3.0 and collected into a vessel previously spiked with 1 part 0.5 M Na ₂ HPO ₄ per every 10 parts collected volume. Fractions are analyzed by SDS-PAGE.

HIC polishing: To separate N-terminal variants (the four residues at the absolute N-terminus are not essential for protein-L binding) and full conformational variants, hydrophobic interaction chromatography (HIC) is used. HIC stationary phase (GE Capto Phenyl ImpRes), HIC mobile phase A (20 mM histidine, 0.02% (w/v) polysorbate 80, pH 6.5±0.1) and HIC mobile phase B (1 M ammonium sulfate, 20 mM histidine, 0.02% (w/v) polysorbate 80, pH 6.5±0.1) is used herein. The column is equilibrated with HIC mobile phase B. The adjusted protein-L eluate is loaded onto a HIC column targeting 2 g/L-resin and traced with HIC mobile phase B until the absorbance at 280 nm (A280) returns to the (local) baseline. Wash the column with 50% B. Bound material is eluted over 75 CV with a 50% B to 0% B gradient. When A280 > 3 mAU (local) above baseline, fractions are collected in 1 CV aliquots. Elution fractions are analyzed based on SE-HPLC and HI-HPLC and combined.

Formulation: The product is exchanged into a formulation buffer, and anion exchange is again used to capture the C-terminal XTEN to bring the product to a target concentration (0.5 g/L). AEX2 stationary phase (GE Q Sepharose FF), AEX2 mobile phase A (20 mM histidine, 40 mM NaCl, 0.02% (w/v) polysorbate 80, pH 6.5±0.2), AEX2 mobile phase B (20 mM histidine, 1 M NaCl, 0.02% (w/v) polysorbate 80, pH 6.5±0.2) and AEX2 mobile phase C (12.2 mM Na ₂ HPO ₄ , 7.8 mM Na ₂ HPO ₄ , 40 mM NaCl, 0.02% (w/v) poly Sorbate 80, pH 7.0±0.2) is used herein. The column is equilibrated with AEX2 mobile phase C. The HIC pool was adjusted to pH 7.0±0.1 and 7±1 mS/cm (using MQ), loaded onto an AEX2 column with a target of 2 g/L-resin, and AEX2 until A280 returned to (local) baseline. Follow up with mobile phase C. The column is washed with AEX2 mobile phase A (20 mM histidine, 40 mM NaCl, 0.02% (w/v) polysorbate 80, pH 6.5±0.2). A [NaCl] step is created using AEX2 mobile phases A and B and elution is performed. The bound material is eluted stepwise to 38% AEX2 mobile phase B. AEX2 eluate collection is initiated when A280 > 5 mAU (local) above baseline and terminated once 2 CVs have been collected. The AEX2 eluate is 0.22 μm filtered in BSC, aliquoted, labeled and stored at -80°C as bulk drug substance (BDS). Bulk drug substance (BDS) is validated by a variety of analytical methods to ensure that all lot release criteria are met. Overall quality is analyzed by SDS-PAGE, ratios of monomers to dimers and aggregates are analyzed by SE-HPLC, and N-terminal quality and product homogeneity are analyzed by HI-HPLC.

Example 2 Preparation of Plasma Samples

This example describes the preparation of a plasma sample from a patient suffering from or suspected of suffering from a disease or condition known to be associated with elevated levels of elastin at or near the diseased site.

Blood of selected patients is collected in EDTA plasma tubes and centrifuged at 4° C. and 3,500 g for 10 minutes. Plasma is then aliquoted and snap-frozen on dry ice within 30 minutes of collection. A 250 μL aliquot of plasma is later thawed on ice and precipitated with 1 mL of water containing 80% acetonitrile and 1 nanogram (ng) of bovine insulin as an internal standard. After the solid phase extraction eluate was transferred and evaporated to dryness, it was diluted with 75 μL of water containing 0.1% formic acid to obtain a plasma peptide sample.

Possible modifications in sample preparation, including for nano LC/MS, are described in Kay et al. 2018 ( Rapid Communications in Mass Spectrometry 32 (16), 1414-1424, 2018).

Example 3 Liquid Chromatography-Mass Spectrometry (LC-MS)

This example describes a liquid chromatography-mass spectroscopy (LC-MS) method used to determine the presence and/or amount of a biomarker peptide in a plasma sample from a subject using the methods disclosed herein.

50 μL of plasma peptides obtained according to Example 2 are injected into a liquid chromatography-mass spectrometry (LC-MS) system in a high flow configuration. Prepare two buffers for liquid chromatography (LC) separations, buffer A (0.1% formic acid in water) and buffer B (80:20 acetonitrile/0.1% formic acid in water). 50 μL of the sample extract is injected onto an HSS T3 column (2.1 x 50 mm) in 15% Buffer A and 85% Buffer B at a flow rate of 300 μL/min, then separated using a 6.5 min gradient to 40% Buffer B. . The column is then washed in 90% Buffer B for 1.5 minutes and returned to initial conditions after 8 minutes. Scans from 600 mass (m/z) per charge to 1,600 m/z are performed for information-dependent acquisition using a resolution of 75,000, maximum charge time of 200 ms, and automatic gain control of 3 × 10 ⁶ .

Peptides are identified using Peaks 8.0 software searched against the human Swissprot database. The search configuration included precursor and product ion tolerances of 10 ppm and 0.05 Da (respectively), a no digestion setting, a false discovery rate threshold of 1%, and tolerances for modifications such as C-terminal amidation.

Example 4 Matrix Assisted Laser Desorption/Ionization-Time-of-Flight (MALDI-TOF) Mass Spectrometry

This example describes a matrix-assisted laser desorption/ionization-time-of-flight (MALDI-TOF) mass spectrometry method used to determine the presence and/or amount of a biomarker peptide in a plasma sample from a subject using the methods disclosed herein. explain

As an alternative to Example 3 , the plasma peptides obtained according to Example 2 were prepared according to Bedin et al. 2015 (J Cell Physiol., 231(4):915-25) on nanoporous silica chips for analysis by matrix-assisted laser desorption/ionization-time-of-flight (MALDI-TOF) mass spectrometry. A plasma sample mixed with a solution of 20% acetonitrile and 1% trifluoroacetic acid in a 3:1 ratio was loaded and isolated. Plasma peptides are identified using Mascot and MS-Tag search engines and preprocessing steps performed by flexAnalysis and SnapTM software. Plasma having (i) the sequence of GVAPGIGPGG (as shown in #527 of column IV of Table A ), or (ii) the sequence of VAAAAKSAAK (SEQ ID NO: 3116; as shown in #527 of column VI of Table A ) (or a fragment thereof). The presence or/and amount of the peptide is determined.

Example 5 Enzyme-Linked Immunosorbent Assay (ELISA)

This example describes an immunoassay used to determine the presence and/or amount of a biomarker peptide in a plasma sample from a subject using the methods disclosed herein.

(i) the sequence of GVAPGIGPGG (SEQ ID NO ) (shown in #527 of column IV of Table A ), (ii) the sequence of VAAAAKSAAK (SEQ ID NO ) (shown in #527 of column VI of Table A ) and (iii) GPGGVAAA A capture antibody specific for one or more biomarker(s) of the sequence (SEQ ID NO: ) (shown in #527 of column II of Table A ) (or a fragment thereof) is obtained.

Plasma samples obtained according to Example 2 are diluted and plasma concentrations of the biomarker peptide(s) are measured using competitive ELISA. A primary antibody (unlabeled) is incubated with the sample antigen. The antibody-antigen complexes are then added to a 96-well plate pre-coated with the same antigen. The plate is washed to remove unbound antibody. (The more antigen in the sample, the less antibody can bind to the antigen in the well, thus "competition".) Add a secondary antibody specific to the primary antibody and conjugated with an enzyme. Substrate is added, and the remaining enzyme induces a chromogenic or fluorescent signal.

Example 6 Patient Designation

This example illustrates the designation of patients likely to respond to an activatable therapeutic using the methods disclosed herein.

The presence or/and amount of biomarker peptide(s) as determined according to one of Examples 3-5 is assayed manually or with a semi-automated/automated procedure/instrument. If the biomarker peptide(s) are determined to be present in a plasma sample from the patient, or if the amount of the patient's biomarker peptide(s) is determined to exceed a pre-determined threshold, the patient is assigned an elastin-based protein in the release segment. It is assigned a greater than 50% probability of responding to a therapeutic agent constructed and produced according to Example 1 comprising the peptide substrate (indicated in #527 of column II of Table A ).

Example 7. Assessment of protease cleavage of collagen I derived release segments

amino acid sequence

The present invention provides non-natural activatable therapeutics (eg, XPAT), wherein the biologically active moiety (BM) is a mammalian protease that cleaves a cleavable bond in the release segment directly or indirectly linked to the BM. It is preferentially released at the target site involved in expression. Successful therapeutic use of these agents in an individual depends on whether the agents contain a release segment linked directly or indirectly to the BM that is cleaved by a mammalian protease expressed at the target site of the individual. Assessment of whether an individual having a target site to be targeted for delivery and release of BM expresses a mammalian protease that cleaves the release segment can be useful in identifying and matching therapeutically effective agents for a particular individual. Achieving such informative assessments will depend on determining the relative efficiency of cleavage of release segment sequences by mammalian proteases known to be expressed at therapeutic target sites, such as tumors and sites of inflammation.

Presented in this example are experimental results demonstrating the unmasking rate of ECP-based emission sites. Substrates 818-P1, C1MA and C1MB were digested with proteases and cleavage rates were measured.

Protease digestion was performed under various conditions and was based on a comparison of 818-P1 digestion with 818-C1MA and 818-C1MB. As shown in Table 8, substrates (1 μM) were digested at 37°C with MMP for 2 hours, legumain and ST14 for 4 hours, or urokinase-type plasminogen activator (uPA) for 6 hours. . Digestion buffers varied in composition and enzyme concentration, MMP (5 nM), legumain, ST14 (50 nM) and uPA (100 nM). Cleavage of 818-P1, C1MA and C1MB at lysine/leucine residues similar to collagen (a known component of the extracellular matrix, ECM) is illustrated in FIG. 9 .

The results demonstrated that MMPs 2, 7 and 9 unmasked 818-P1 faster than 818-C1MA and 818-C1MB (MMP2: 818-P1 > 818-C1MA > 818-C1MB; MMP7: 818-P1 > 818-C1MB). C1MA = 818-C1MB; MMP9: 818-P1 > 818-C1MB > 818-C1MA). Legumain and ST 14 required higher concentrations and longer time for demasking. ST14 demasking was characterized by 818-C1MA > 818-P1 > 818-C1MB, while legumain showed minimal demasking differences. The unmasking activity due to uPA required a higher concentration of protease and a longer digestion time.

Proteases expressed during cancer growth and metastasis can remodel the ECM and lead to elevated plasma levels of ECM protein cleavage products elevated in the plasma of patients with various tumors. This example demonstrates that the cleavage products resulting from MMP cleavage of ECM proteins are very similar to the MMP cleavage sites of linkers cleavable by proteases in XPAT. These results show that the protease cleavable linker used in the XPAT of the present invention is cleaved more efficiently than ECM by purified MMP, and the presence of ECM peptides in cancer patients is given by cleavage of the linker cleavable by protease in XPAT. By predicting whether a patient or tumor can cleave XPAT, it has been demonstrated that MMPs capable of treating tumors can act as an indicator that a patient's tumor is expressing. This enables a personalized approach to determining whether XPAT will be cleaved in a given tumor type by determining whether a subject with that tumor type has high plasma levels of a particular cleavage product(s) derived from the extracellular matrix.

Table 8. Protease sources and partial digestion conditions

Table 9. Protease Cleavage Release Segment Sequences

Although preferred embodiments of the present invention have been illustrated and described herein, it will be apparent to those skilled in the art that these embodiments are provided by way of example only. It is not intended that the present invention be limited by the specific examples provided within the specification. Although the present invention has been described with reference to the foregoing specification, the description and illustration of the embodiments herein are not meant to be construed in a limiting sense. Numerous variations, alterations, and substitutions will now occur to those skilled in the art without departing from the invention. It is also to be understood that all aspects of the present invention are not limited to the specific depictions, configurations or relative proportions set forth herein which depend on various conditions and variables. It should be understood that various alternatives to the embodiments of the invention described herein may be used in practicing the invention. Accordingly, the present invention is contemplated to cover any such alternatives, modifications, variations or equivalents. It is intended that the following claims define the scope of the invention and that methods and structures within the scope of these claims and their equivalents be embraced therein.

SEQUENCE LISTING <110> Amunix Pharmaceuticals Inc. Schellenberger, Volker Rennerfeldt, Deena Henkensiefken, Angela To, Milton <120> COMPOSITIONS AND METHODS RELATED TO ACTIVATABLE THERAPEUTIC AGENTS <130> 20-1831-WO <150> 63/054525 <151> 2020-07-21 <160> 3129 <170> PatentIn version 3.5 <210> 1 <211> 16 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1 Gly Pro Gly Gly Val Ala Ala Ala Val Ser Lys Arg Phe Pro Val Gly 1 5 10 15 <210> 2 <211> 16 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2 Gly Val Arg Gly Leu Thr Gly Pro Val Ser Lys Arg Phe Pro Val Gly 1 5 10 15 <210> 3 <211> 16 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3 Val Ser Lys Arg Phe Pro Val Gly Glu Ala Gly Arg Ser Ala Asn His 1 5 10 15 <210> 4 <211> 16 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 4 Glu Ala Gly Arg Ser Ala Asn His Gly Val Arg Gly Leu Thr Gly Pro 1 5 10 15 <210> 5 <211> 16 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 5 Glu Ala Gly Arg Ser Ala Asn His Thr Pro Ala Gly Leu Thr Gly Pro 1 5 10 15 <210> 6 <211> 16 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 6 Ser Pro Glu Ala Gln Ala Ala Ala Glu Ala Gly Arg Ser Ala Asn His 1 5 10 15 <210> 7 <211> 16 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 7 Gln Pro Ala His Leu Thr Phe Pro Glu Ala Gly Arg Ser Ala Asn His 1 5 10 15 <210> 8 <211> 15 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 8 Ala Gly Ser Pro Gly Lys Asp Gly Val Arg Gly Leu Thr Gly Pro 1 5 10 15 <210> 9 <211> 1445 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 9 Ala Ser His His His His His His Ser Pro Ala Gly Ser Pro Thr Ser 1 5 10 15 Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 20 25 30 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 35 40 45 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 50 55 60 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 65 70 75 80 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 85 90 95 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 100 105 110 Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 115 120 125 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 130 135 140 Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 145 150 155 160 Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 165 170 175 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu 180 185 190 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 195 200 205 Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 210 215 220 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 225 230 235 240 Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 245 250 255 Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 260 265 270 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 275 280 285 Pro Ser Glu Gly Ser Ala Pro Gly Gly Ser Ala Pro Gly Pro Ser Gly 290 295 300 His Met Gly Arg Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Asp Ile 305 310 315 320 Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly Asp Arg 325 330 335 Val Thr Ile Thr Cys Lys Ala Ser Gln Asp Val Ser Ile Gly Val Ala 340 345 350 Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile Tyr Ser 355 360 365 Ala Ser Tyr Arg Tyr Thr Gly Val Pro Ser Arg Phe Ser Gly Ser Gly 370 375 380 Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln Pro Glu Asp 385 390 395 400 Phe Ala Thr Tyr Tyr Cys Gln Gln Tyr Tyr Ile Tyr Pro Tyr Thr Phe 405 410 415 Gly Gln Gly Thr Lys Val Glu Ile Lys Gly Ala Thr Pro Pro Glu Thr 420 425 430 Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr Gly Gly Ser Ala Glu 435 440 445 Ser Glu Pro Pro Gly Glu Gly Glu Val Gln Leu Val Glu Ser Gly Gly 450 455 460 Gly Leu Val Gln Pro Gly Gly Ser Leu Arg Leu Ser Cys Ala Ala Ser 465 470 475 480 Gly Phe Thr Phe Thr Asp Tyr Thr Met Asp Trp Val Arg Gln Ala Pro 485 490 495 Gly Lys Gly Leu Glu Trp Val Ala Asp Val Asn Pro Asn Ser Gly Gly 500 505 510 Ser Ile Tyr Asn Gln Arg Phe Lys Gly Arg Phe Thr Leu Ser Val Asp 515 520 525 Arg Ser Lys Asn Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Ala Glu 530 535 540 Asp Thr Ala Val Tyr Cys Ala Arg Asn Leu Gly Pro Ser Phe Tyr 545 550 555 560 Phe Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 565 570 575 Gly Gly Ser Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser 580 585 590 Pro Gly Gly Thr Val Thr Leu Thr Cys Arg Ser Ser Asn Gly Ala Val 595 600 605 Thr Ser Ser Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala 610 615 620 Pro Arg Gly Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr Pro 625 630 635 640 Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu 645 650 655 Ser Gly Val Gln Pro Glu Asp Glu Ala Val Tyr Tyr Cys Ala Leu Trp 660 665 670 Tyr Pro Asn Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 675 680 685 Gly Ala Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu 690 695 700 Thr Thr Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu Val 705 710 715 720 Gln Leu Leu Glu Ser Gly Gly Gly Ile Val Gln Pro Gly Gly Ser Leu 725 730 735 Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr Ala Met 740 745 750 Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg 755 760 765 Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Ser Val 770 775 780 Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Val Tyr 785 790 795 800 Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys 805 810 815 Val Arg His Glu Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe Ala His 820 825 830 Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Thr Ala Glu Ala 835 840 845 Ala Ser Ala Ser Gly Gly Pro Ser Gly His Met Gly Arg Pro Gly Ser 850 855 860 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala 865 870 875 880 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 885 890 895 Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr 900 905 910 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 915 920 925 Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 930 935 940 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser 945 950 955 960 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser 965 970 975 Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 980 985 990 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 995 1000 1005 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly 1010 1015 1020 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu 1025 1030 1035 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1040 1045 1050 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1055 1060 1065 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 1070 1075 1080 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1085 1090 1095 Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1100 1105 1110 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1115 1120 1125 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser 1130 1135 1140 Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr 1145 1150 1155 Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1160 1165 1170 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 1175 1180 1185 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu 1190 1195 1200 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 1205 1210 1215 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1220 1225 1230 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1235 1240 1245 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 1250 1255 1260 Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 1265 1270 1275 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1280 1285 1290 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser 1295 1300 1305 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 1310 1315 1320 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1325 1330 1335 Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1340 1345 1350 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1355 1360 1365 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly 1370 1375 1380 Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr 1385 1390 1395 Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 1400 1405 1410 Glu Ser Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1415 1420 1425 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ala Ala Glu Pro 1430 1435 1440 Glu Ala 1445 <210> 10 <211> 1445 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 10 Ala Ser His His His His His His Ser Pro Ala Gly Ser Pro Thr Ser 1 5 10 15 Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 20 25 30 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 35 40 45 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 50 55 60 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 65 70 75 80 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 85 90 95 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 100 105 110 Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 115 120 125 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 130 135 140 Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 145 150 155 160 Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 165 170 175 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu 180 185 190 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 195 200 205 Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 210 215 220 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 225 230 235 240 Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 245 250 255 Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 260 265 270 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 275 280 285 Pro Ser Glu Gly Ser Ala Pro Gly Gly Ser Ala Pro His Pro Val Glu 290 295 300 Leu Leu Ala Arg Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Asp Ile 305 310 315 320 Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly Asp Arg 325 330 335 Val Thr Ile Thr Cys Gln Ala Ser Gln Asp Ile Ser Asn Tyr Leu Asn 340 345 350 Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile Tyr Asp 355 360 365 Ala Ser Asn Leu Glu Thr Gly Val Pro Ser Arg Phe Ser Gly Ser Gly 370 375 380 Ser Gly Thr Asp Phe Thr Phe Thr Ile Ser Ser Leu Gln Pro Glu Asp 385 390 395 400 Ile Ala Thr Tyr Phe Cys Gln His Phe Asp His Leu Pro Leu Ala Phe 405 410 415 Gly Gly Gly Thr Lys Val Glu Ile Lys Gly Ala Thr Pro Pro Glu Thr 420 425 430 Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr Gly Gly Ser Ala Glu 435 440 445 Ser Glu Pro Pro Gly Glu Gly Gln Val Gln Leu Gln Glu Ser Gly Pro 450 455 460 Gly Leu Val Lys Pro Ser Glu Thr Leu Ser Leu Thr Cys Thr Val Ser 465 470 475 480 Gly Gly Ser Val Ser Ser Gly Asp Tyr Tyr Trp Thr Trp Ile Arg Gln 485 490 495 Ser Pro Gly Lys Gly Leu Glu Trp Ile Gly His Ile Tyr Tyr Ser Gly 500 505 510 Asn Thr Asn Tyr Asn Pro Ser Leu Lys Ser Arg Leu Thr Ile Ser Ile 515 520 525 Asp Thr Ser Lys Thr Gln Phe Ser Leu Lys Leu Ser Ser Val Thr Ala 530 535 540 Ala Asp Thr Ala Ile Tyr Tyr Cys Val Arg Asp Arg Val Thr Gly Ala 545 550 555 560 Phe Asp Ile Trp Gly Gln Gly Thr Met Val Thr Val Ser Ser Gly Gly 565 570 575 Gly Gly Ser Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser 580 585 590 Pro Gly Gly Thr Val Thr Leu Thr Cys Arg Ser Ser Thr Gly Ala Val 595 600 605 Thr Thr Ser Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala 610 615 620 Pro Arg Gly Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr Pro 625 630 635 640 Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu 645 650 655 Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Ala Leu Trp 660 665 670 Tyr Ser Asn Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 675 680 685 Gly Ala Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu 690 695 700 Thr Thr Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu Val 705 710 715 720 Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 725 730 735 Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr Ala Met 740 745 750 Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg 755 760 765 Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Ser Val 770 775 780 Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr 785 790 795 800 Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys 805 810 815 Val Arg His Gly Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe Ala Tyr 820 825 830 Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Thr Ala Glu Ala 835 840 845 Ala Ser Ala Ser Gly His Pro Val Glu Leu Leu Ala Arg Pro Gly Ser 850 855 860 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala 865 870 875 880 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 885 890 895 Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr 900 905 910 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 915 920 925 Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 930 935 940 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser 945 950 955 960 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser 965 970 975 Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 980 985 990 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 995 1000 1005 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly 1010 1015 1020 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu 1025 1030 1035 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1040 1045 1050 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1055 1060 1065 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 1070 1075 1080 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1085 1090 1095 Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1100 1105 1110 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1115 1120 1125 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser 1130 1135 1140 Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr 1145 1150 1155 Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1160 1165 1170 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 1175 1180 1185 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu 1190 1195 1200 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 1205 1210 1215 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1220 1225 1230 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1235 1240 1245 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 1250 1255 1260 Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 1265 1270 1275 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1280 1285 1290 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser 1295 1300 1305 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 1310 1315 1320 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1325 1330 1335 Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1340 1345 1350 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1355 1360 1365 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly 1370 1375 1380 Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr 1385 1390 1395 Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 1400 1405 1410 Glu Ser Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1415 1420 1425 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ala Ala Glu Pro 1430 1435 1440 Glu Ala 1445 <210> 11 <211> 1445 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 11 Ala Ser His His His His His His Ser Pro Ala Gly Ser Pro Thr Ser 1 5 10 15 Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 20 25 30 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 35 40 45 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 50 55 60 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 65 70 75 80 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 85 90 95 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 100 105 110 Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 115 120 125 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 130 135 140 Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 145 150 155 160 Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 165 170 175 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu 180 185 190 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 195 200 205 Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 210 215 220 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 225 230 235 240 Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 245 250 255 Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 260 265 270 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 275 280 285 Pro Ser Glu Gly Ser Ala Pro Gly Gly Ser Ala Pro Val Ser Lys Arg 290 295 300 Phe Pro Val Gly Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Asp Ile 305 310 315 320 Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly Asp Arg 325 330 335 Val Thr Ile Thr Cys Gln Ala Ser Gln Asp Ile Ser Asn Tyr Leu Asn 340 345 350 Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile Tyr Asp 355 360 365 Ala Ser Asn Leu Glu Thr Gly Val Pro Ser Arg Phe Ser Gly Ser Gly 370 375 380 Ser Gly Thr Asp Phe Thr Phe Thr Ile Ser Ser Leu Gln Pro Glu Asp 385 390 395 400 Ile Ala Thr Tyr Phe Cys Gln His Phe Asp His Leu Pro Leu Ala Phe 405 410 415 Gly Gly Gly Thr Lys Val Glu Ile Lys Gly Ala Thr Pro Pro Glu Thr 420 425 430 Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr Gly Gly Ser Ala Glu 435 440 445 Ser Glu Pro Pro Gly Glu Gly Gln Val Gln Leu Gln Glu Ser Gly Pro 450 455 460 Gly Leu Val Lys Pro Ser Glu Thr Leu Ser Leu Thr Cys Thr Val Ser 465 470 475 480 Gly Gly Ser Val Ser Ser Gly Asp Tyr Tyr Trp Thr Trp Ile Arg Gln 485 490 495 Ser Pro Gly Lys Gly Leu Glu Trp Ile Gly His Ile Tyr Tyr Ser Gly 500 505 510 Asn Thr Asn Tyr Asn Pro Ser Leu Lys Ser Arg Leu Thr Ile Ser Ile 515 520 525 Asp Thr Ser Lys Thr Gln Phe Ser Leu Lys Leu Ser Ser Val Thr Ala 530 535 540 Ala Asp Thr Ala Ile Tyr Tyr Cys Val Arg Asp Arg Val Thr Gly Ala 545 550 555 560 Phe Asp Ile Trp Gly Gln Gly Thr Met Val Thr Val Ser Ser Gly Gly 565 570 575 Gly Gly Ser Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser 580 585 590 Pro Gly Gly Thr Val Thr Leu Thr Cys Arg Ser Ser Thr Gly Ala Val 595 600 605 Thr Thr Ser Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala 610 615 620 Pro Arg Gly Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr Pro 625 630 635 640 Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu 645 650 655 Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Ala Leu Trp 660 665 670 Tyr Ser Asn Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 675 680 685 Gly Ala Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu 690 695 700 Thr Thr Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu Val 705 710 715 720 Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 725 730 735 Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr Ala Met 740 745 750 Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg 755 760 765 Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Ser Val 770 775 780 Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr 785 790 795 800 Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys 805 810 815 Val Arg His Gly Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe Ala Tyr 820 825 830 Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Thr Ala Glu Ala 835 840 845 Ala Ser Ala Ser Gly Val Ser Lys Arg Phe Pro Val Gly Pro Gly Ser 850 855 860 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala 865 870 875 880 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 885 890 895 Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr 900 905 910 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 915 920 925 Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 930 935 940 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser 945 950 955 960 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser 965 970 975 Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 980 985 990 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 995 1000 1005 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly 1010 1015 1020 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu 1025 1030 1035 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1040 1045 1050 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1055 1060 1065 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 1070 1075 1080 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1085 1090 1095 Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1100 1105 1110 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1115 1120 1125 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser 1130 1135 1140 Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr 1145 1150 1155 Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1160 1165 1170 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 1175 1180 1185 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu 1190 1195 1200 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 1205 1210 1215 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1220 1225 1230 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1235 1240 1245 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 1250 1255 1260 Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 1265 1270 1275 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1280 1285 1290 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser 1295 1300 1305 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 1310 1315 1320 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1325 1330 1335 Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1340 1345 1350 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1355 1360 1365 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly 1370 1375 1380 Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr 1385 1390 1395 Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 1400 1405 1410 Glu Ser Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1415 1420 1425 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ala Ala Glu Pro 1430 1435 1440 Glu Ala 1445 <210> 12 <211> 1446 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 12 Ala Ser Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Ser Gly Thr Ser 1 5 10 15 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Glu Thr Glu Pro Ser 20 25 30 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 35 40 45 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 50 55 60 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Thr Pro Ala Glu Ser 65 70 75 80 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 85 90 95 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 100 105 110 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 115 120 125 Pro Glu Ser Gly Pro Gly Glu Ser Pro Ala Thr Ser Gly Ser Thr Pro 130 135 140 Glu Ser Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro 145 150 155 160 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro 165 170 175 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 180 185 190 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 195 200 205 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 210 215 220 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 225 230 235 240 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro 245 250 255 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 260 265 270 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 275 280 285 Pro Gly Gly Ser Ala Pro Glu Ala Gly Arg Ser Ala Asn His Thr Pro 290 295 300 Ala Gly Leu Thr Gly Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 305 310 315 320 Glu Ile Val Leu Thr Gln Ser Pro Ala Thr Leu Ser Leu Ser Pro Gly 325 330 335 Glu Arg Ala Thr Leu Ser Cys Lys Ala Ser Gln Asp Val Ser Ile Gly 340 345 350 Val Ala Trp Tyr Gln Gln Lys Pro Gly Gln Ala Pro Arg Leu Leu Ile 355 360 365 Tyr Ser Ala Ser Tyr Arg Tyr Ser Gly Val Pro Ala Arg Phe Ser Gly 370 375 380 Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Glu Pro 385 390 395 400 Glu Asp Phe Ala Val Tyr Tyr Cys Gln Gln Tyr Tyr Ile Tyr Pro Tyr 405 410 415 Thr Phe Gly Gln Gly Thr Lys Val Glu Ile Lys Gly Ala Thr Pro Pro 420 425 430 Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr Gly Gly Ser 435 440 445 Ala Glu Ser Glu Pro Pro Gly Glu Gly Gln Val Gln Leu Val Gln Ser 450 455 460 Gly Val Glu Val Lys Lys Pro Gly Ala Ser Val Lys Val Ser Cys Lys 465 470 475 480 Ala Ser Gly Phe Thr Phe Thr Asp Tyr Thr Met Asp Trp Val Arg Gln 485 490 495 Ala Pro Gly Gln Gly Leu Glu Trp Met Ala Asp Val Asn Pro Asn Ser 500 505 510 Gly Gly Ser Ile Tyr Asn Gln Arg Phe Lys Gly Arg Val Thr Leu Thr 515 520 525 Thr Asp Ser Ser Thr Thr Thr Thr Ala Tyr Met Glu Leu Lys Ser Leu Gln 530 535 540 Phe Asp Asp Thr Ala Val Tyr Tyr Cys Ala Arg Asn Leu Gly Pro Ser 545 550 555 560 Phe Tyr Phe Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 565 570 575 Gly Gly Gly Ser Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val 580 585 590 Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Arg Ser Ser Asn Gly Ala 595 600 605 Val Thr Ser Ser Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln 610 615 620 Ala Pro Arg Gly Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr 625 630 635 640 Pro Ala Arg Phe Ser Gly Ser Ser Leu Gly Gly Lys Ala Ala Leu Thr 645 650 655 Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Val Tyr Tyr Cys Ala Leu 660 665 670 Trp Tyr Pro Asn Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val 675 680 685 Leu Gly Ala Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly 690 695 700 Glu Thr Thr Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu 705 710 715 720 Val Gln Leu Gln Glu Ser Gly Gly Gly Ile Val Gln Pro Gly Gly Ser 725 730 735 Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr Ala 740 745 750 Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala 755 760 765 Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Ser 770 775 780 Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Val 785 790 795 800 Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr 805 810 815 Cys Val Arg His Glu Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe Ala 820 825 830 His Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Thr Ala Glu 835 840 845 Ala Ala Ser Ala Ser Gly Glu Ala Gly Arg Ser Ala Asn His Thr Pro 850 855 860 Ala Gly Leu Thr Gly Pro Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu 865 870 875 880 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr 885 890 895 Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 900 905 910 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu 915 920 925 Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu 930 935 940 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 945 950 955 960 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 965 970 975 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 980 985 990 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 995 1000 1005 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 1010 1015 1020 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala 1025 1030 1035 Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 1040 1045 1050 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 1055 1060 1065 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 1070 1075 1080 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro 1085 1090 1095 Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 1100 1105 1110 Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 1115 1120 1125 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro 1130 1135 1140 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala 1145 1150 1155 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 1160 1165 1170 Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 1175 1180 1185 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 1190 1195 1200 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr 1205 1210 1215 Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 1220 1225 1230 Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 1235 1240 1245 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 1250 1255 1260 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr 1265 1270 1275 Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 1280 1285 1290 Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 1295 1300 1305 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 1310 1315 1320 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala 1325 1330 1335 Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 1340 1345 1350 Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 1355 1360 1365 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu 1370 1375 1380 Ser Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser 1385 1390 1395 Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly 1400 1405 1410 Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 1415 1420 1425 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 1430 1435 1440 Glu Ser Ala 1445 <210> 13 <211> 1445 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 13 Ala Ser His His His His His His Ser Pro Ala Gly Ser Pro Thr Ser 1 5 10 15 Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 20 25 30 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 35 40 45 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 50 55 60 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 65 70 75 80 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 85 90 95 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 100 105 110 Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 115 120 125 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 130 135 140 Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 145 150 155 160 Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 165 170 175 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu 180 185 190 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 195 200 205 Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 210 215 220 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 225 230 235 240 Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 245 250 255 Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 260 265 270 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 275 280 285 Pro Ser Glu Gly Ser Ala Pro Gly Gly Ser Ala Pro Ser Pro Glu Ala 290 295 300 Gln Ala Ala Ala Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Asp Ile 305 310 315 320 Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly Asp Arg 325 330 335 Val Thr Ile Thr Cys Gln Ala Ser Gln Asp Ile Ser Asn Tyr Leu Asn 340 345 350 Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile Tyr Asp 355 360 365 Ala Ser Asn Leu Glu Thr Gly Val Pro Ser Arg Phe Ser Gly Ser Gly 370 375 380 Ser Gly Thr Asp Phe Thr Phe Thr Ile Ser Ser Leu Gln Pro Glu Asp 385 390 395 400 Ile Ala Thr Tyr Phe Cys Gln His Phe Asp His Leu Pro Leu Ala Phe 405 410 415 Gly Gly Gly Thr Lys Val Glu Ile Lys Gly Ala Thr Pro Pro Glu Thr 420 425 430 Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr Gly Gly Ser Ala Glu 435 440 445 Ser Glu Pro Pro Gly Glu Gly Gln Val Gln Leu Gln Glu Ser Gly Pro 450 455 460 Gly Leu Val Lys Pro Ser Glu Thr Leu Ser Leu Thr Cys Thr Val Ser 465 470 475 480 Gly Gly Ser Val Ser Ser Gly Asp Tyr Tyr Trp Thr Trp Ile Arg Gln 485 490 495 Ser Pro Gly Lys Gly Leu Glu Trp Ile Gly His Ile Tyr Tyr Ser Gly 500 505 510 Asn Thr Asn Tyr Asn Pro Ser Leu Lys Ser Arg Leu Thr Ile Ser Ile 515 520 525 Asp Thr Ser Lys Thr Gln Phe Ser Leu Lys Leu Ser Ser Val Thr Ala 530 535 540 Ala Asp Thr Ala Ile Tyr Tyr Cys Val Arg Asp Arg Val Thr Gly Ala 545 550 555 560 Phe Asp Ile Trp Gly Gln Gly Thr Met Val Thr Val Ser Ser Gly Gly 565 570 575 Gly Gly Ser Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser 580 585 590 Pro Gly Gly Thr Val Thr Leu Thr Cys Arg Ser Ser Thr Gly Ala Val 595 600 605 Thr Thr Ser Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala 610 615 620 Pro Arg Gly Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr Pro 625 630 635 640 Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu 645 650 655 Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Ala Leu Trp 660 665 670 Tyr Ser Asn Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 675 680 685 Gly Ala Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu 690 695 700 Thr Thr Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu Val 705 710 715 720 Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 725 730 735 Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr Ala Met 740 745 750 Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg 755 760 765 Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Ser Val 770 775 780 Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr 785 790 795 800 Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys 805 810 815 Val Arg His Gly Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe Ala Tyr 820 825 830 Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Thr Ala Glu Ala 835 840 845 Ala Ser Ala Ser Gly Ser Pro Glu Ala Gln Ala Ala Ala Pro Gly Ser 850 855 860 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala 865 870 875 880 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 885 890 895 Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr 900 905 910 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 915 920 925 Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 930 935 940 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser 945 950 955 960 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser 965 970 975 Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 980 985 990 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 995 1000 1005 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly 1010 1015 1020 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu 1025 1030 1035 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1040 1045 1050 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1055 1060 1065 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 1070 1075 1080 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1085 1090 1095 Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1100 1105 1110 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1115 1120 1125 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser 1130 1135 1140 Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr 1145 1150 1155 Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1160 1165 1170 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 1175 1180 1185 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu 1190 1195 1200 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 1205 1210 1215 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1220 1225 1230 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1235 1240 1245 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 1250 1255 1260 Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 1265 1270 1275 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1280 1285 1290 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser 1295 1300 1305 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 1310 1315 1320 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1325 1330 1335 Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1340 1345 1350 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1355 1360 1365 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly 1370 1375 1380 Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr 1385 1390 1395 Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 1400 1405 1410 Glu Ser Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1415 1420 1425 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ala Ala Glu Pro 1430 1435 1440 Glu Ala 1445 <210> 14 <211> 1461 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 14 Ala Ser His His His His His His Ser Pro Ala Gly Ser Pro Thr Ser 1 5 10 15 Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 20 25 30 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 35 40 45 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 50 55 60 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 65 70 75 80 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 85 90 95 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 100 105 110 Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 115 120 125 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 130 135 140 Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 145 150 155 160 Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 165 170 175 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu 180 185 190 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 195 200 205 Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 210 215 220 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 225 230 235 240 Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 245 250 255 Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 260 265 270 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 275 280 285 Pro Ser Glu Gly Ser Ala Pro Gly Gly Ser Ala Pro Glu Ala Gly Arg 290 295 300 Ser Ala Asn His Gly Val Arg Gly Leu Thr Gly Pro Ala Thr Ser Gly 305 310 315 320 Ser Glu Thr Pro Gly Thr Asp Ile Gln Met Thr Gln Ser Pro Ser Ser 325 330 335 Leu Ser Ala Ser Val Gly Asp Arg Val Thr Ile Thr Cys Lys Ala Ser 340 345 350 Gln Asp Val Ser Ile Gly Val Ala Trp Tyr Gln Gln Lys Pro Gly Lys 355 360 365 Ala Pro Lys Leu Leu Ile Tyr Ser Ala Ser Tyr Arg Tyr Thr Gly Val 370 375 380 Pro Ser Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr 385 390 395 400 Ile Ser Ser Leu Gln Pro Glu Asp Phe Ala Thr Tyr Tyr Cys Gln Gln 405 410 415 Tyr Tyr Ile Tyr Pro Tyr Thr Phe Gly Gln Gly Thr Lys Val Glu Ile 420 425 430 Lys Gly Ala Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly 435 440 445 Glu Thr Thr Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu 450 455 460 Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser 465 470 475 480 Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Thr Asp Tyr Thr 485 490 495 Met Asp Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala 500 505 510 Asp Val Asn Pro Asn Ser Gly Gly Ser Ile Tyr Asn Gln Arg Phe Lys 515 520 525 Gly Arg Phe Thr Leu Ser Val Asp Arg Ser Lys Asn Thr Leu Tyr Leu 530 535 540 Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala 545 550 555 560 Arg Asn Leu Gly Pro Ser Phe Tyr Phe Asp Tyr Trp Gly Gln Gly Thr 565 570 575 Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Glu Leu Val Val Thr 580 585 590 Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr 595 600 605 Cys Arg Ser Ser Asn Gly Ala Val Thr Ser Ser Asn Tyr Ala Asn Trp 610 615 620 Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr 625 630 635 640 Asn Lys Arg Ala Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 645 650 655 Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu 660 665 670 Ala Val Tyr Tyr Cys Ala Leu Trp Tyr Pro Asn Leu Trp Val Phe Gly 675 680 685 Gly Gly Thr Lys Leu Thr Val Leu Gly Ala Thr Pro Pro Glu Thr Gly 690 695 700 Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr Gly Gly Ser Ala Glu Ser 705 710 715 720 Glu Pro Pro Gly Glu Gly Glu Val Gln Leu Leu Glu Ser Gly Gly Gly 725 730 735 Ile Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly 740 745 750 Phe Thr Phe Asn Thr Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly 755 760 765 Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr 770 775 780 Ala Thr Tyr Tyr Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg 785 790 795 800 Asp Asp Ser Lys Asn Thr Val Tyr Leu Gln Met Asn Asn Leu Lys Thr 805 810 815 Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Glu Asn Phe Gly Asn 820 825 830 Ser Tyr Val Ser Trp Phe Ala His Trp Gly Gln Gly Thr Leu Val Thr 835 840 845 Val Ser Ser Gly Thr Ala Glu Ala Ala Ser Ala Ser Gly Glu Ala Gly 850 855 860 Arg Ser Ala Asn His Gly Val Arg Gly Leu Thr Gly Pro Pro Gly Ser 865 870 875 880 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala 885 890 895 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 900 905 910 Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr 915 920 925 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 930 935 940 Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 945 950 955 960 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser 965 970 975 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser 980 985 990 Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 995 1000 1005 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 1010 1015 1020 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala 1025 1030 1035 Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 1040 1045 1050 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 1055 1060 1065 Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 1070 1075 1080 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu 1085 1090 1095 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 1100 1105 1110 Gly Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 1115 1120 1125 Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 1130 1135 1140 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu 1145 1150 1155 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro 1160 1165 1170 Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 1175 1180 1185 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly 1190 1195 1200 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr 1205 1210 1215 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 1220 1225 1230 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 1235 1240 1245 Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 1250 1255 1260 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 1265 1270 1275 Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 1280 1285 1290 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 1295 1300 1305 Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 1310 1315 1320 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu 1325 1330 1335 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 1340 1345 1350 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 1355 1360 1365 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 1370 1375 1380 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala 1385 1390 1395 Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro 1400 1405 1410 Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr 1415 1420 1425 Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 1430 1435 1440 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ala Ala Glu 1445 1450 1455 Pro Glu Ala 1460 <210> 15 <211> 1445 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 15 Ala Ser His His His His His His Ser Pro Ala Gly Ser Pro Thr Ser 1 5 10 15 Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 20 25 30 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 35 40 45 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 50 55 60 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 65 70 75 80 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 85 90 95 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 100 105 110 Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 115 120 125 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 130 135 140 Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 145 150 155 160 Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 165 170 175 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu 180 185 190 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 195 200 205 Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 210 215 220 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 225 230 235 240 Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 245 250 255 Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 260 265 270 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 275 280 285 Pro Ser Glu Gly Ser Ala Pro Gly Gly Ser Ala Pro Leu Thr Ser Asp 290 295 300 Leu Gln Ala Gln Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Asp Ile 305 310 315 320 Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly Asp Arg 325 330 335 Val Thr Ile Thr Cys Lys Ala Ser Gln Asp Val Ser Ile Gly Val Ala 340 345 350 Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile Tyr Ser 355 360 365 Ala Ser Tyr Arg Tyr Thr Gly Val Pro Ser Arg Phe Ser Gly Ser Gly 370 375 380 Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln Pro Glu Asp 385 390 395 400 Phe Ala Thr Tyr Tyr Cys Gln Gln Tyr Tyr Ile Tyr Pro Tyr Thr Phe 405 410 415 Gly Gln Gly Thr Lys Val Glu Ile Lys Gly Ala Thr Pro Pro Glu Thr 420 425 430 Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr Gly Gly Ser Ala Glu 435 440 445 Ser Glu Pro Pro Gly Glu Gly Glu Val Gln Leu Val Glu Ser Gly Gly 450 455 460 Gly Leu Val Gln Pro Gly Gly Ser Leu Arg Leu Ser Cys Ala Ala Ser 465 470 475 480 Gly Phe Thr Phe Thr Asp Tyr Thr Met Asp Trp Val Arg Gln Ala Pro 485 490 495 Gly Lys Gly Leu Glu Trp Val Ala Asp Val Asn Pro Asn Ser Gly Gly 500 505 510 Ser Ile Tyr Asn Gln Arg Phe Lys Gly Arg Phe Thr Leu Ser Val Asp 515 520 525 Arg Ser Lys Asn Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Ala Glu 530 535 540 Asp Thr Ala Val Tyr Cys Ala Arg Asn Leu Gly Pro Ser Phe Tyr 545 550 555 560 Phe Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 565 570 575 Gly Gly Ser Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser 580 585 590 Pro Gly Gly Thr Val Thr Leu Thr Cys Arg Ser Ser Asn Gly Ala Val 595 600 605 Thr Ser Ser Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala 610 615 620 Pro Arg Gly Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr Pro 625 630 635 640 Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu 645 650 655 Ser Gly Val Gln Pro Glu Asp Glu Ala Val Tyr Tyr Cys Ala Leu Trp 660 665 670 Tyr Pro Asn Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 675 680 685 Gly Ala Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu 690 695 700 Thr Thr Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu Val 705 710 715 720 Gln Leu Leu Glu Ser Gly Gly Gly Ile Val Gln Pro Gly Gly Ser Leu 725 730 735 Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr Ala Met 740 745 750 Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg 755 760 765 Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Ser Val 770 775 780 Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Val Tyr 785 790 795 800 Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys 805 810 815 Val Arg His Glu Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe Ala His 820 825 830 Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Thr Ala Glu Ala 835 840 845 Ala Ser Ala Ser Gly Leu Thr Ser Asp Leu Gln Ala Gln Pro Gly Ser 850 855 860 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala 865 870 875 880 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 885 890 895 Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr 900 905 910 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 915 920 925 Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 930 935 940 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser 945 950 955 960 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser 965 970 975 Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 980 985 990 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 995 1000 1005 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly 1010 1015 1020 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu 1025 1030 1035 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1040 1045 1050 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1055 1060 1065 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 1070 1075 1080 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1085 1090 1095 Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1100 1105 1110 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1115 1120 1125 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser 1130 1135 1140 Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr 1145 1150 1155 Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1160 1165 1170 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 1175 1180 1185 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu 1190 1195 1200 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 1205 1210 1215 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1220 1225 1230 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1235 1240 1245 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 1250 1255 1260 Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 1265 1270 1275 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1280 1285 1290 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser 1295 1300 1305 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 1310 1315 1320 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1325 1330 1335 Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1340 1345 1350 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1355 1360 1365 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly 1370 1375 1380 Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr 1385 1390 1395 Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 1400 1405 1410 Glu Ser Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1415 1420 1425 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ala Ala Glu Pro 1430 1435 1440 Glu Ala 1445 <210> 16 <211> 1445 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 16 Ala Ser His His His His His His Ser Pro Ala Gly Ser Pro Thr Ser 1 5 10 15 Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 20 25 30 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 35 40 45 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 50 55 60 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 65 70 75 80 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 85 90 95 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 100 105 110 Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 115 120 125 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 130 135 140 Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 145 150 155 160 Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 165 170 175 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu 180 185 190 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 195 200 205 Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 210 215 220 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 225 230 235 240 Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 245 250 255 Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 260 265 270 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 275 280 285 Pro Ser Glu Gly Ser Ala Pro Gly Gly Ser Ala Pro Gln Pro Val Ser 290 295 300 Leu Ala Asn Thr Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Asp Ile 305 310 315 320 Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly Asp Arg 325 330 335 Val Thr Ile Thr Cys Lys Ala Ser Gln Asp Val Ser Ile Gly Val Ala 340 345 350 Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile Tyr Ser 355 360 365 Ala Ser Tyr Arg Tyr Thr Gly Val Pro Ser Arg Phe Ser Gly Ser Gly 370 375 380 Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln Pro Glu Asp 385 390 395 400 Phe Ala Thr Tyr Tyr Cys Gln Gln Tyr Tyr Ile Tyr Pro Tyr Thr Phe 405 410 415 Gly Gln Gly Thr Lys Val Glu Ile Lys Gly Ala Thr Pro Pro Glu Thr 420 425 430 Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr Gly Gly Ser Ala Glu 435 440 445 Ser Glu Pro Pro Gly Glu Gly Glu Val Gln Leu Val Glu Ser Gly Gly 450 455 460 Gly Leu Val Gln Pro Gly Gly Ser Leu Arg Leu Ser Cys Ala Ala Ser 465 470 475 480 Gly Phe Thr Phe Thr Asp Tyr Thr Met Asp Trp Val Arg Gln Ala Pro 485 490 495 Gly Lys Gly Leu Glu Trp Val Ala Asp Val Asn Pro Asn Ser Gly Gly 500 505 510 Ser Ile Tyr Asn Gln Arg Phe Lys Gly Arg Phe Thr Leu Ser Val Asp 515 520 525 Arg Ser Lys Asn Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Ala Glu 530 535 540 Asp Thr Ala Val Tyr Cys Ala Arg Asn Leu Gly Pro Ser Phe Tyr 545 550 555 560 Phe Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 565 570 575 Gly Gly Ser Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser 580 585 590 Pro Gly Gly Thr Val Thr Leu Thr Cys Arg Ser Ser Asn Gly Ala Val 595 600 605 Thr Ser Ser Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala 610 615 620 Pro Arg Gly Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr Pro 625 630 635 640 Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu 645 650 655 Ser Gly Val Gln Pro Glu Asp Glu Ala Val Tyr Tyr Cys Ala Leu Trp 660 665 670 Tyr Pro Asn Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 675 680 685 Gly Ala Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu 690 695 700 Thr Thr Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu Val 705 710 715 720 Gln Leu Leu Glu Ser Gly Gly Gly Ile Val Gln Pro Gly Gly Ser Leu 725 730 735 Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr Ala Met 740 745 750 Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg 755 760 765 Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Ser Val 770 775 780 Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Val Tyr 785 790 795 800 Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys 805 810 815 Val Arg His Glu Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe Ala His 820 825 830 Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Thr Ala Glu Ala 835 840 845 Ala Ser Ala Ser Gly Gln Pro Val Ser Leu Ala Asn Thr Pro Gly Ser 850 855 860 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala 865 870 875 880 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 885 890 895 Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr 900 905 910 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 915 920 925 Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 930 935 940 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser 945 950 955 960 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser 965 970 975 Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 980 985 990 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 995 1000 1005 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly 1010 1015 1020 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu 1025 1030 1035 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1040 1045 1050 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1055 1060 1065 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 1070 1075 1080 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1085 1090 1095 Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1100 1105 1110 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1115 1120 1125 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser 1130 1135 1140 Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr 1145 1150 1155 Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1160 1165 1170 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 1175 1180 1185 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu 1190 1195 1200 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 1205 1210 1215 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1220 1225 1230 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1235 1240 1245 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 1250 1255 1260 Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 1265 1270 1275 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1280 1285 1290 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser 1295 1300 1305 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 1310 1315 1320 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1325 1330 1335 Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1340 1345 1350 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1355 1360 1365 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly 1370 1375 1380 Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr 1385 1390 1395 Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 1400 1405 1410 Glu Ser Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1415 1420 1425 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ala Ala Glu Pro 1430 1435 1440 Glu Ala 1445 <210> 17 <211> 1445 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 17 Ala Ser His His His His His His Ser Pro Ala Gly Ser Pro Thr Ser 1 5 10 15 Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 20 25 30 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 35 40 45 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 50 55 60 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 65 70 75 80 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 85 90 95 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 100 105 110 Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 115 120 125 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 130 135 140 Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 145 150 155 160 Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 165 170 175 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu 180 185 190 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 195 200 205 Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 210 215 220 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 225 230 235 240 Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 245 250 255 Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 260 265 270 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 275 280 285 Pro Ser Glu Gly Ser Ala Pro Gly Gly Ser Ala Pro Gly Val Arg Gly 290 295 300 Leu Thr Gly Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Asp Ile 305 310 315 320 Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly Asp Arg 325 330 335 Val Thr Ile Thr Cys Lys Ala Ser Gln Asp Val Ser Ile Gly Val Ala 340 345 350 Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile Tyr Ser 355 360 365 Ala Ser Tyr Arg Tyr Thr Gly Val Pro Ser Arg Phe Ser Gly Ser Gly 370 375 380 Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln Pro Glu Asp 385 390 395 400 Phe Ala Thr Tyr Tyr Cys Gln Gln Tyr Tyr Ile Tyr Pro Tyr Thr Phe 405 410 415 Gly Gln Gly Thr Lys Val Glu Ile Lys Gly Ala Thr Pro Pro Glu Thr 420 425 430 Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr Gly Gly Ser Ala Glu 435 440 445 Ser Glu Pro Pro Gly Glu Gly Glu Val Gln Leu Val Glu Ser Gly Gly 450 455 460 Gly Leu Val Gln Pro Gly Gly Ser Leu Arg Leu Ser Cys Ala Ala Ser 465 470 475 480 Gly Phe Thr Phe Thr Asp Tyr Thr Met Asp Trp Val Arg Gln Ala Pro 485 490 495 Gly Lys Gly Leu Glu Trp Val Ala Asp Val Asn Pro Asn Ser Gly Gly 500 505 510 Ser Ile Tyr Asn Gln Arg Phe Lys Gly Arg Phe Thr Leu Ser Val Asp 515 520 525 Arg Ser Lys Asn Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Ala Glu 530 535 540 Asp Thr Ala Val Tyr Cys Ala Arg Asn Leu Gly Pro Ser Phe Tyr 545 550 555 560 Phe Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 565 570 575 Gly Gly Ser Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser 580 585 590 Pro Gly Gly Thr Val Thr Leu Thr Cys Arg Ser Ser Asn Gly Ala Val 595 600 605 Thr Ser Ser Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala 610 615 620 Pro Arg Gly Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr Pro 625 630 635 640 Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu 645 650 655 Ser Gly Val Gln Pro Glu Asp Glu Ala Val Tyr Tyr Cys Ala Leu Trp 660 665 670 Tyr Pro Asn Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 675 680 685 Gly Ala Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu 690 695 700 Thr Thr Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu Val 705 710 715 720 Gln Leu Leu Glu Ser Gly Gly Gly Ile Val Gln Pro Gly Gly Ser Leu 725 730 735 Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr Ala Met 740 745 750 Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg 755 760 765 Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Ser Val 770 775 780 Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Val Tyr 785 790 795 800 Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys 805 810 815 Val Arg His Glu Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe Ala His 820 825 830 Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Thr Ala Glu Ala 835 840 845 Ala Ser Ala Ser Gly Gly Val Arg Gly Leu Thr Gly Pro Pro Gly Ser 850 855 860 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala 865 870 875 880 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 885 890 895 Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr 900 905 910 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 915 920 925 Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 930 935 940 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser 945 950 955 960 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser 965 970 975 Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 980 985 990 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 995 1000 1005 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly 1010 1015 1020 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu 1025 1030 1035 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1040 1045 1050 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1055 1060 1065 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 1070 1075 1080 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1085 1090 1095 Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1100 1105 1110 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1115 1120 1125 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser 1130 1135 1140 Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr 1145 1150 1155 Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1160 1165 1170 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 1175 1180 1185 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu 1190 1195 1200 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 1205 1210 1215 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1220 1225 1230 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1235 1240 1245 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 1250 1255 1260 Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 1265 1270 1275 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1280 1285 1290 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser 1295 1300 1305 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 1310 1315 1320 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1325 1330 1335 Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1340 1345 1350 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1355 1360 1365 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly 1370 1375 1380 Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr 1385 1390 1395 Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 1400 1405 1410 Glu Ser Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1415 1420 1425 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ala Ala Glu Pro 1430 1435 1440 Glu Ala 1445 <210> 18 <211> 2304 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 18 Ser Ala Gly Ser Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 1 5 10 15 Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 20 25 30 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 35 40 45 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 50 55 60 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 65 70 75 80 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Thr Pro Ala Glu Ser 85 90 95 Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 100 105 110 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 115 120 125 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 130 135 140 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 145 150 155 160 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 165 170 175 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 180 185 190 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 195 200 205 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 210 215 220 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 225 230 235 240 Gly Ser Thr Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 245 250 255 Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 260 265 270 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala 275 280 285 Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr 290 295 300 Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser 305 310 315 320 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala 325 330 335 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 340 345 350 Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 355 360 365 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 370 375 380 Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 385 390 395 400 Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser 405 410 415 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro 420 425 430 Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 435 440 445 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 450 455 460 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr 465 470 475 480 Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 485 490 495 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 500 505 510 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser 515 520 525 Pro Thr Ser Thr Glu Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr 530 535 540 Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly Thr 545 550 555 560 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro 565 570 575 Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 580 585 590 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 595 600 605 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr 610 615 620 Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 625 630 635 640 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser 645 650 655 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala 660 665 670 Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu 675 680 685 Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser 690 695 700 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly Ser Pro Ala Gly Ser 705 710 715 720 Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 725 730 735 Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 740 745 750 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala 755 760 765 Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu 770 775 780 Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser 785 790 795 800 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro 805 810 815 Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 820 825 830 Ala Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 835 840 845 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro 850 855 860 Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr 865 870 875 880 Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 885 890 895 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser 900 905 910 Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 915 920 925 Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 930 935 940 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr 945 950 955 960 Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu 965 970 975 Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr 980 985 990 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro 995 1000 1005 Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 1010 1015 1020 Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 1025 1030 1035 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 1040 1045 1050 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala 1055 1060 1065 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 1070 1075 1080 Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 1085 1090 1095 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 1100 1105 1110 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 1115 1120 1125 Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 1130 1135 1140 Ser Gly Pro Gly Thr Glu Ser Ala Ser Ala Ser Gly Arg Ala Ala 1145 1150 1155 Asn Glu Thr Pro Pro Gly Leu Thr Gly Ala Ala Thr Ser Gly Ser 1160 1165 1170 Glu Thr Pro Gly Thr Glu Ile Val Leu Thr Gln Ser Pro Ala Thr 1175 1180 1185 Leu Ser Leu Ser Pro Gly Glu Arg Ala Thr Leu Ser Cys Lys Ala 1190 1195 1200 Ser Gln Asp Val Ser Ile Gly Val Ala Trp Tyr Gln Gln Lys Pro 1205 1210 1215 Gly Gln Ala Pro Arg Leu Leu Ile Tyr Ser Ala Ser Tyr Arg Tyr 1220 1225 1230 Ser Gly Val Pro Ala Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp 1235 1240 1245 Phe Thr Leu Thr Ile Ser Ser Leu Glu Pro Glu Asp Phe Ala Val 1250 1255 1260 Tyr Tyr Cys Gln Gln Tyr Tyr Ile Tyr Pro Tyr Thr Phe Gly Gln 1265 1270 1275 Gly Thr Lys Val Glu Ile Lys Gly Ala Thr Pro Pro Glu Thr Gly 1280 1285 1290 Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr Gly Gly Ser Ala Glu 1295 1300 1305 Ser Glu Pro Pro Gly Glu Gly Gln Val Gln Leu Val Gln Ser Gly 1310 1315 1320 Val Glu Val Lys Lys Pro Gly Ala Ser Val Lys Val Ser Cys Lys 1325 1330 1335 Ala Ser Gly Phe Thr Phe Thr Asp Tyr Thr Met Asp Trp Val Arg 1340 1345 1350 Gln Ala Pro Gly Gln Gly Leu Glu Trp Met Ala Asp Val Asn Pro 1355 1360 1365 Asn Ser Gly Gly Ser Ile Tyr Asn Gln Arg Phe Lys Gly Arg Val 1370 1375 1380 Thr Leu Thr Thr Asp Ser Ser Thr Thr Thr Thr Ala Tyr Met Glu Leu 1385 1390 1395 Lys Ser Leu Gln Phe Asp Asp Thr Ala Val Tyr Tyr Cys Ala Arg 1400 1405 1410 Asn Leu Gly Pro Ser Phe Tyr Phe Asp Tyr Trp Gly Gln Gly Thr 1415 1420 1425 Leu Val Thr Val Ser Ser Gly Gly Gly Ser Glu Leu Val Val Thr 1430 1435 1440 Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu 1445 1450 1455 Thr Cys Arg Ser Ser Asn Gly Ala Val Thr Ser Ser Asn Tyr Ala 1460 1465 1470 Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile 1475 1480 1485 Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr Pro Ala Arg Phe Ser 1490 1495 1500 Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val 1505 1510 1515 Gln Pro Glu Asp Glu Ala Val Tyr Tyr Cys Ala Leu Trp Tyr Pro 1520 1525 1530 Asn Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly 1535 1540 1545 Ala Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu 1550 1555 1560 Thr Thr Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu 1565 1570 1575 Val Gln Leu Leu Glu Ser Gly Gly Gly Ile Val Gln Pro Gly Gly 1580 1585 1590 Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr 1595 1600 1605 Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu 1610 1615 1620 Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr 1625 1630 1635 Tyr Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp 1640 1645 1650 Ser Lys Asn Thr Val Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu 1655 1660 1665 Asp Thr Ala Val Tyr Tyr Cys Val Arg His Glu Asn Phe Gly Asn 1670 1675 1680 Ser Tyr Val Ser Trp Phe Ala His Trp Gly Gln Gly Thr Leu Val 1685 1690 1695 Thr Val Ser Ser Gly Thr Ala Glu Ala Ala Ser Ala Ser Gly Ala 1700 1705 1710 Ser Gly Arg Ala Ala Asn Glu Thr Pro Pro Gly Leu Thr Gly Ala 1715 1720 1725 Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr 1730 1735 1740 Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 1745 1750 1755 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 1760 1765 1770 Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 1775 1780 1785 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 1790 1795 1800 Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 1805 1810 1815 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr 1820 1825 1830 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 1835 1840 1845 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu 1850 1855 1860 Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 1865 1870 1875 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu 1880 1885 1890 Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 1895 1900 1905 Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr 1910 1915 1920 Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 1925 1930 1935 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu 1940 1945 1950 Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 1955 1960 1965 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 1970 1975 1980 Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 1985 1990 1995 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 2000 2005 2010 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 2015 2020 2025 Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr 2030 2035 2040 Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 2045 2050 2055 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro 2060 2065 2070 Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 2075 2080 2085 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu 2090 2095 2100 Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 2105 2110 2115 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu 2120 2125 2130 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro 2135 2140 2145 Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr 2150 2155 2160 Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly 2165 2170 2175 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr 2180 2185 2190 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 2195 2200 2205 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Thr 2210 2215 2220 Glu Thr Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 2225 2230 2235 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu 2240 2245 2250 Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 2255 2260 2265 Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr 2270 2275 2280 Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 2285 2290 2295 Ser Glu Pro Ala Thr Ser 2300 <210> 19 <211> 2030 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 19 Ala Ser Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Ser Gly Thr Ser 1 5 10 15 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Glu Thr Glu Pro Ser 20 25 30 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 35 40 45 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 50 55 60 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Thr Pro Ala Glu Ser 65 70 75 80 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 85 90 95 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 100 105 110 Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly Thr Ser Glu Ser Ala Thr 115 120 125 Pro Glu Ser Gly Pro Gly Glu Ser Pro Ala Thr Ser Gly Ser Thr Pro 130 135 140 Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro 145 150 155 160 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro 165 170 175 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 180 185 190 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 195 200 205 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 210 215 220 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 225 230 235 240 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro 245 250 255 Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly Thr Ser Thr Glu Pro Ser 260 265 270 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 275 280 285 Pro Gly Gly Ser Ala Pro Thr Thr Gly Arg Ala Gly Glu Ala Ala Asn 290 295 300 Ala Thr Ser Ala Gly Ala Thr Gly Pro Ala Thr Ser Gly Ser Glu Thr 305 310 315 320 Pro Gly Thr Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala 325 330 335 Ser Val Gly Asp Arg Val Thr Ile Thr Cys Arg Ala Ser Gln Asp Val 340 345 350 Asn Thr Ala Val Ala Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys 355 360 365 Leu Leu Ile Tyr Ser Ala Ser Phe Leu Tyr Ser Gly Val Pro Ser Arg 370 375 380 Phe Ser Gly Ser Arg Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Ser 385 390 395 400 Leu Gln Pro Glu Asp Phe Ala Thr Tyr Tyr Cys Gln Gln His Tyr Thr 405 410 415 Thr Pro Pro Thr Phe Gly Gln Gly Thr Lys Val Glu Ile Lys Gly Ala 420 425 430 Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr 435 440 445 Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu Val Gln Leu 450 455 460 Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Arg Leu 465 470 475 480 Ser Cys Ala Ala Ser Gly Phe Asn Ile Lys Asp Thr Tyr Ile His Trp 485 490 495 Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Tyr 500 505 510 Pro Thr Asn Gly Tyr Thr Arg Tyr Ala Asp Ser Val Lys Gly Arg Phe 515 520 525 Thr Ile Ser Ala Asp Thr Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn 530 535 540 Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ser Arg Trp Gly 545 550 555 560 Gly Asp Gly Phe Tyr Ala Met Asp Tyr Trp Gly Gln Gly Thr Leu Val 565 570 575 Thr Val Ser Ser Gly Gly Gly Ser Glu Leu Val Val Thr Gln Glu Pro 580 585 590 Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Arg Ser 595 600 605 Ser Asn Gly Ala Val Thr Ser Ser Asn Tyr Ala Asn Trp Val Gln Gln 610 615 620 Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Asn Lys Arg 625 630 635 640 Ala Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Gly Lys 645 650 655 Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Val Tyr 660 665 670 Tyr Cys Ala Leu Trp Tyr Pro Asn Leu Trp Val Phe Gly Gly Gly Thr 675 680 685 Lys Leu Thr Val Leu Gly Ala Thr Pro Pro Glu Thr Gly Ala Glu Thr 690 695 700 Glu Ser Pro Gly Glu Thr Thr Gly Gly Ser Ala Glu Ser Glu Pro Pro 705 710 715 720 Gly Glu Gly Glu Val Gln Leu Leu Glu Ser Gly Gly Gly Ile Val Gln 725 730 735 Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe 740 745 750 Asn Thr Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu 755 760 765 Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr 770 775 780 Tyr Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser 785 790 795 800 Lys Asn Thr Val Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr 805 810 815 Ala Val Tyr Tyr Cys Val Arg His Glu Asn Phe Gly Asn Ser Tyr Val 820 825 830 Ser Trp Phe Ala His Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 835 840 845 Gly Thr Ala Glu Ala Ala Ser Ala Ser Gly Thr Thr Gly Arg Ala Gly 850 855 860 Glu Ala Ala Asn Ala Thr Ser Ala Gly Ala Thr Gly Pro Ser Ala Gly 865 870 875 880 Ser Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr 885 890 895 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro 900 905 910 Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr 915 920 925 Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 930 935 940 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala 945 950 955 960 Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu 965 970 975 Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser 980 985 990 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala 995 1000 1005 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 1010 1015 1020 Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 1025 1030 1035 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 1040 1045 1050 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 1055 1060 1065 Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 1070 1075 1080 Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 1085 1090 1095 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 1100 1105 1110 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro 1115 1120 1125 Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 1130 1135 1140 Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 1145 1150 1155 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro 1160 1165 1170 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala 1175 1180 1185 Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 1190 1195 1200 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 1205 1210 1215 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 1220 1225 1230 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 1235 1240 1245 Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 1250 1255 1260 Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 1265 1270 1275 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 1280 1285 1290 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro 1295 1300 1305 Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 1310 1315 1320 Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 1325 1330 1335 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 1340 1345 1350 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala 1355 1360 1365 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 1370 1375 1380 Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 1385 1390 1395 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro 1400 1405 1410 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser 1415 1420 1425 Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu 1430 1435 1440 Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 1445 1450 1455 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 1460 1465 1470 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala 1475 1480 1485 Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 1490 1495 1500 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 1505 1510 1515 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 1520 1525 1530 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala 1535 1540 1545 Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 1550 1555 1560 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 1565 1570 1575 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro 1580 1585 1590 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro 1595 1600 1605 Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 1610 1615 1620 Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 1625 1630 1635 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 1640 1645 1650 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr 1655 1660 1665 Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser 1670 1675 1680 Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 1685 1690 1695 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Glu 1700 1705 1710 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala 1715 1720 1725 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 1730 1735 1740 Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 1745 1750 1755 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 1760 1765 1770 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser 1775 1780 1785 Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly 1790 1795 1800 Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 1805 1810 1815 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 1820 1825 1830 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr 1835 1840 1845 Ser Gly Ser Thr Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr 1850 1855 1860 Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1865 1870 1875 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1880 1885 1890 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly 1895 1900 1905 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu 1910 1915 1920 Gly Ser Ala Pro Gly Thr Ala Thr Glu Ser Pro Glu Gly Ser Ala 1925 1930 1935 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1940 1945 1950 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Ala Glu 1955 1960 1965 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 1970 1975 1980 Gly Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 1985 1990 1995 Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 2000 2005 2010 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Glu Ser 2015 2020 2025 Ala Ser 2030 <210> 20 <211> 1445 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 20 Ala Ser His His His His His His Ser Pro Ala Gly Ser Pro Thr Ser 1 5 10 15 Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 20 25 30 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 35 40 45 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 50 55 60 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 65 70 75 80 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 85 90 95 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 100 105 110 Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 115 120 125 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 130 135 140 Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 145 150 155 160 Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 165 170 175 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu 180 185 190 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 195 200 205 Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 210 215 220 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 225 230 235 240 Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 245 250 255 Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 260 265 270 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 275 280 285 Pro Ser Glu Gly Ser Ala Pro Gly Gly Ser Ala Pro Gly Pro Gly Gly 290 295 300 Val Ala Ala Ala Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Asp Ile 305 310 315 320 Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly Asp Arg 325 330 335 Val Thr Ile Thr Cys Lys Ala Ser Gln Asp Val Ser Ile Gly Val Ala 340 345 350 Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile Tyr Ser 355 360 365 Ala Ser Tyr Arg Tyr Thr Gly Val Pro Ser Arg Phe Ser Gly Ser Gly 370 375 380 Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln Pro Glu Asp 385 390 395 400 Phe Ala Thr Tyr Tyr Cys Gln Gln Tyr Tyr Ile Tyr Pro Tyr Thr Phe 405 410 415 Gly Gln Gly Thr Lys Val Glu Ile Lys Gly Ala Thr Pro Pro Glu Thr 420 425 430 Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr Gly Gly Ser Ala Glu 435 440 445 Ser Glu Pro Pro Gly Glu Gly Glu Val Gln Leu Val Glu Ser Gly Gly 450 455 460 Gly Leu Val Gln Pro Gly Gly Ser Leu Arg Leu Ser Cys Ala Ala Ser 465 470 475 480 Gly Phe Thr Phe Thr Asp Tyr Thr Met Asp Trp Val Arg Gln Ala Pro 485 490 495 Gly Lys Gly Leu Glu Trp Val Ala Asp Val Asn Pro Asn Ser Gly Gly 500 505 510 Ser Ile Tyr Asn Gln Arg Phe Lys Gly Arg Phe Thr Leu Ser Val Asp 515 520 525 Arg Ser Lys Asn Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Ala Glu 530 535 540 Asp Thr Ala Val Tyr Cys Ala Arg Asn Leu Gly Pro Ser Phe Tyr 545 550 555 560 Phe Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 565 570 575 Gly Gly Ser Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser 580 585 590 Pro Gly Gly Thr Val Thr Leu Thr Cys Arg Ser Ser Asn Gly Ala Val 595 600 605 Thr Ser Ser Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala 610 615 620 Pro Arg Gly Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr Pro 625 630 635 640 Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu 645 650 655 Ser Gly Val Gln Pro Glu Asp Glu Ala Val Tyr Tyr Cys Ala Leu Trp 660 665 670 Tyr Pro Asn Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 675 680 685 Gly Ala Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu 690 695 700 Thr Thr Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu Val 705 710 715 720 Gln Leu Leu Glu Ser Gly Gly Gly Ile Val Gln Pro Gly Gly Ser Leu 725 730 735 Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr Ala Met 740 745 750 Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg 755 760 765 Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Ser Val 770 775 780 Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Val Tyr 785 790 795 800 Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys 805 810 815 Val Arg His Glu Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe Ala His 820 825 830 Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Thr Ala Glu Ala 835 840 845 Ala Ser Ala Ser Gly Gly Pro Gly Gly Val Ala Ala Ala Pro Gly Ser 850 855 860 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala 865 870 875 880 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 885 890 895 Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr 900 905 910 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 915 920 925 Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 930 935 940 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser 945 950 955 960 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser 965 970 975 Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 980 985 990 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 995 1000 1005 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly 1010 1015 1020 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu 1025 1030 1035 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1040 1045 1050 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1055 1060 1065 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 1070 1075 1080 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1085 1090 1095 Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1100 1105 1110 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1115 1120 1125 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser 1130 1135 1140 Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr 1145 1150 1155 Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1160 1165 1170 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 1175 1180 1185 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu 1190 1195 1200 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 1205 1210 1215 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1220 1225 1230 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1235 1240 1245 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 1250 1255 1260 Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 1265 1270 1275 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1280 1285 1290 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser 1295 1300 1305 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 1310 1315 1320 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1325 1330 1335 Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1340 1345 1350 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1355 1360 1365 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly 1370 1375 1380 Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr 1385 1390 1395 Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 1400 1405 1410 Glu Ser Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1415 1420 1425 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ala Ala Glu Pro 1430 1435 1440 Glu Ala 1445 <210> 21 <211> 1445 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 21 Ala Ser His His His His His His Ser Pro Ala Gly Ser Pro Thr Ser 1 5 10 15 Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 20 25 30 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 35 40 45 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 50 55 60 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 65 70 75 80 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 85 90 95 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 100 105 110 Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 115 120 125 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 130 135 140 Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 145 150 155 160 Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 165 170 175 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu 180 185 190 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 195 200 205 Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 210 215 220 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 225 230 235 240 Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 245 250 255 Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 260 265 270 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 275 280 285 Pro Ser Glu Gly Ser Ala Pro Gly Gly Ser Ala Pro Val Ser Lys Arg 290 295 300 Phe Pro Val Gly Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Asp Ile 305 310 315 320 Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly Asp Arg 325 330 335 Val Thr Ile Thr Cys Lys Ala Ser Gln Asp Val Ser Ile Gly Val Ala 340 345 350 Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile Tyr Ser 355 360 365 Ala Ser Tyr Arg Tyr Thr Gly Val Pro Ser Arg Phe Ser Gly Ser Gly 370 375 380 Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln Pro Glu Asp 385 390 395 400 Phe Ala Thr Tyr Tyr Cys Gln Gln Tyr Tyr Ile Tyr Pro Tyr Thr Phe 405 410 415 Gly Gln Gly Thr Lys Val Glu Ile Lys Gly Ala Thr Pro Pro Glu Thr 420 425 430 Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr Gly Gly Ser Ala Glu 435 440 445 Ser Glu Pro Pro Gly Glu Gly Glu Val Gln Leu Val Glu Ser Gly Gly 450 455 460 Gly Leu Val Gln Pro Gly Gly Ser Leu Arg Leu Ser Cys Ala Ala Ser 465 470 475 480 Gly Phe Thr Phe Thr Asp Tyr Thr Met Asp Trp Val Arg Gln Ala Pro 485 490 495 Gly Lys Gly Leu Glu Trp Val Ala Asp Val Asn Pro Asn Ser Gly Gly 500 505 510 Ser Ile Tyr Asn Gln Arg Phe Lys Gly Arg Phe Thr Leu Ser Val Asp 515 520 525 Arg Ser Lys Asn Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Ala Glu 530 535 540 Asp Thr Ala Val Tyr Cys Ala Arg Asn Leu Gly Pro Ser Phe Tyr 545 550 555 560 Phe Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 565 570 575 Gly Gly Ser Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser 580 585 590 Pro Gly Gly Thr Val Thr Leu Thr Cys Arg Ser Ser Asn Gly Ala Val 595 600 605 Thr Ser Ser Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala 610 615 620 Pro Arg Gly Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr Pro 625 630 635 640 Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu 645 650 655 Ser Gly Val Gln Pro Glu Asp Glu Ala Val Tyr Tyr Cys Ala Leu Trp 660 665 670 Tyr Pro Asn Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 675 680 685 Gly Ala Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu 690 695 700 Thr Thr Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu Val 705 710 715 720 Gln Leu Leu Glu Ser Gly Gly Gly Ile Val Gln Pro Gly Gly Ser Leu 725 730 735 Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr Ala Met 740 745 750 Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg 755 760 765 Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Ser Val 770 775 780 Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Val Tyr 785 790 795 800 Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys 805 810 815 Val Arg His Glu Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe Ala His 820 825 830 Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Thr Ala Glu Ala 835 840 845 Ala Ser Ala Ser Gly Val Ser Lys Arg Phe Pro Val Gly Pro Gly Ser 850 855 860 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala 865 870 875 880 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 885 890 895 Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr 900 905 910 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 915 920 925 Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 930 935 940 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser 945 950 955 960 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser 965 970 975 Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 980 985 990 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 995 1000 1005 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly 1010 1015 1020 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu 1025 1030 1035 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1040 1045 1050 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1055 1060 1065 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 1070 1075 1080 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1085 1090 1095 Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1100 1105 1110 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1115 1120 1125 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser 1130 1135 1140 Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr 1145 1150 1155 Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1160 1165 1170 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 1175 1180 1185 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu 1190 1195 1200 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 1205 1210 1215 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1220 1225 1230 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1235 1240 1245 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 1250 1255 1260 Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 1265 1270 1275 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1280 1285 1290 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser 1295 1300 1305 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 1310 1315 1320 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1325 1330 1335 Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1340 1345 1350 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1355 1360 1365 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly 1370 1375 1380 Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr 1385 1390 1395 Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 1400 1405 1410 Glu Ser Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1415 1420 1425 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ala Ala Glu Pro 1430 1435 1440 Glu Ala 1445 <210> 22 <211> 1445 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 22 Ala Ser His His His His His His Ser Pro Ala Gly Ser Pro Thr Ser 1 5 10 15 Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 20 25 30 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 35 40 45 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 50 55 60 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 65 70 75 80 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 85 90 95 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 100 105 110 Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 115 120 125 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 130 135 140 Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 145 150 155 160 Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 165 170 175 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu 180 185 190 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 195 200 205 Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 210 215 220 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 225 230 235 240 Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 245 250 255 Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 260 265 270 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 275 280 285 Pro Ser Glu Gly Ser Ala Pro Gly Gly Ser Ala Pro Gly Pro Gly Gly 290 295 300 Val Ala Ala Ala Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Asp Ile 305 310 315 320 Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly Asp Arg 325 330 335 Val Thr Ile Thr Cys Gln Ala Ser Gln Asp Ile Ser Asn Tyr Leu Asn 340 345 350 Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile Tyr Asp 355 360 365 Ala Ser Asn Leu Glu Thr Gly Val Pro Ser Arg Phe Ser Gly Ser Gly 370 375 380 Ser Gly Thr Asp Phe Thr Phe Thr Ile Ser Ser Leu Gln Pro Glu Asp 385 390 395 400 Ile Ala Thr Tyr Phe Cys Gln His Phe Asp His Leu Pro Leu Ala Phe 405 410 415 Gly Gly Gly Thr Lys Val Glu Ile Lys Gly Ala Thr Pro Pro Glu Thr 420 425 430 Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr Gly Gly Ser Ala Glu 435 440 445 Ser Glu Pro Pro Gly Glu Gly Gln Val Gln Leu Gln Glu Ser Gly Pro 450 455 460 Gly Leu Val Lys Pro Ser Glu Thr Leu Ser Leu Thr Cys Thr Val Ser 465 470 475 480 Gly Gly Ser Val Ser Ser Gly Asp Tyr Tyr Trp Thr Trp Ile Arg Gln 485 490 495 Ser Pro Gly Lys Gly Leu Glu Trp Ile Gly His Ile Tyr Tyr Ser Gly 500 505 510 Asn Thr Asn Tyr Asn Pro Ser Leu Lys Ser Arg Leu Thr Ile Ser Ile 515 520 525 Asp Thr Ser Lys Thr Gln Phe Ser Leu Lys Leu Ser Ser Val Thr Ala 530 535 540 Ala Asp Thr Ala Ile Tyr Tyr Cys Val Arg Asp Arg Val Thr Gly Ala 545 550 555 560 Phe Asp Ile Trp Gly Gln Gly Thr Met Val Thr Val Ser Ser Gly Gly 565 570 575 Gly Gly Ser Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser 580 585 590 Pro Gly Gly Thr Val Thr Leu Thr Cys Arg Ser Ser Thr Gly Ala Val 595 600 605 Thr Thr Ser Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala 610 615 620 Pro Arg Gly Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr Pro 625 630 635 640 Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu 645 650 655 Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Ala Leu Trp 660 665 670 Tyr Ser Asn Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 675 680 685 Gly Ala Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu 690 695 700 Thr Thr Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu Val 705 710 715 720 Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 725 730 735 Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr Ala Met 740 745 750 Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg 755 760 765 Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Ser Val 770 775 780 Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr 785 790 795 800 Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys 805 810 815 Val Arg His Gly Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe Ala Tyr 820 825 830 Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Thr Ala Glu Ala 835 840 845 Ala Ser Ala Ser Gly Gly Pro Gly Gly Val Ala Ala Ala Pro Gly Ser 850 855 860 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala 865 870 875 880 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 885 890 895 Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr 900 905 910 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 915 920 925 Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 930 935 940 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser 945 950 955 960 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser 965 970 975 Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 980 985 990 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 995 1000 1005 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly 1010 1015 1020 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu 1025 1030 1035 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1040 1045 1050 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1055 1060 1065 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 1070 1075 1080 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1085 1090 1095 Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1100 1105 1110 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1115 1120 1125 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser 1130 1135 1140 Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr 1145 1150 1155 Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1160 1165 1170 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 1175 1180 1185 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu 1190 1195 1200 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 1205 1210 1215 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1220 1225 1230 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1235 1240 1245 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 1250 1255 1260 Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 1265 1270 1275 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1280 1285 1290 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser 1295 1300 1305 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 1310 1315 1320 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1325 1330 1335 Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1340 1345 1350 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1355 1360 1365 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly 1370 1375 1380 Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr 1385 1390 1395 Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 1400 1405 1410 Glu Ser Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1415 1420 1425 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ala Ala Glu Pro 1430 1435 1440 Glu Ala 1445 <210> 23 <211> 1449 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 23 Ala Ser Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Ser Gly Thr Ser 1 5 10 15 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 20 25 30 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 35 40 45 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 50 55 60 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Thr Pro Ala Glu Ser 65 70 75 80 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 85 90 95 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 100 105 110 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 115 120 125 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 130 135 140 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro 145 150 155 160 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro 165 170 175 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 180 185 190 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 195 200 205 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 210 215 220 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 225 230 235 240 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro 245 250 255 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 260 265 270 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 275 280 285 Pro Gly Gly Ser Ala Pro Ala Ser Gly Arg Ser Thr Asn Ala Gly Pro 290 295 300 Pro Gly Leu Thr Gly Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 305 310 315 320 Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 325 330 335 Asp Arg Val Thr Ile Thr Cys Arg Ala Ser Gln Asp Val Asn Thr Ala 340 345 350 Val Ala Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile 355 360 365 Tyr Ser Ala Ser Phe Leu Tyr Ser Gly Val Pro Ser Arg Phe Ser Gly 370 375 380 Ser Arg Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln Pro 385 390 395 400 Glu Asp Phe Ala Thr Tyr Tyr Cys Gln Gln His Tyr Thr Thr Pro Pro 405 410 415 Thr Phe Gly Gln Gly Thr Lys Val Glu Ile Lys Gly Ala Thr Pro Pro 420 425 430 Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr Gly Gly Ser 435 440 445 Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu Val Gln Leu Val Glu Ser 450 455 460 Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Arg Leu Ser Cys Ala 465 470 475 480 Ala Ser Gly Phe Asn Ile Lys Asp Thr Tyr Ile His Trp Val Arg Gln 485 490 495 Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Tyr Pro Thr Asn 500 505 510 Gly Tyr Thr Arg Tyr Ala Asp Ser Val Lys Gly Arg Phe Thr Ile Ser 515 520 525 Ala Asp Thr Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Ser Leu Arg 530 535 540 Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ser Arg Trp Gly Gly Asp Gly 545 550 555 560 Phe Tyr Ala Met Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 565 570 575 Ser Gly Gly Gly Ser Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr 580 585 590 Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Arg Ser Ser Thr Gly 595 600 605 Ala Val Thr Thr Ser Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly 610 615 620 Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly 625 630 635 640 Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu 645 650 655 Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Ala 660 665 670 Leu Trp Tyr Ser Asn Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr 675 680 685 Val Leu Gly Ala Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro 690 695 700 Gly Glu Thr Thr Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly 705 710 715 720 Glu Val Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 725 730 735 Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr 740 745 750 Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 755 760 765 Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp 770 775 780 Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr 785 790 795 800 Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr 805 810 815 Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe 820 825 830 Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Thr Ala 835 840 845 Glu Ala Ala Ser Ala Ser Gly Ala Ser Gly Arg Ser Thr Asn Ala Gly 850 855 860 Pro Pro Gly Leu Thr Gly Pro Pro Gly Ser Pro Ala Gly Ser Pro Thr 865 870 875 880 Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 885 890 895 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu 900 905 910 Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu 915 920 925 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 930 935 940 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 945 950 955 960 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 965 970 975 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 980 985 990 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr 995 1000 1005 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 1010 1015 1020 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu 1025 1030 1035 Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 1040 1045 1050 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu 1055 1060 1065 Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 1070 1075 1080 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 1085 1090 1095 Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly 1100 1105 1110 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala 1115 1120 1125 Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 1130 1135 1140 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 1145 1150 1155 Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 1160 1165 1170 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu 1175 1180 1185 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 1190 1195 1200 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 1205 1210 1215 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 1220 1225 1230 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu 1235 1240 1245 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 1250 1255 1260 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 1265 1270 1275 Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly 1280 1285 1290 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr 1295 1300 1305 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 1310 1315 1320 Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 1325 1330 1335 Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 1340 1345 1350 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro 1355 1360 1365 Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro 1370 1375 1380 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 1385 1390 1395 Ala Pro Gly Thr Glu Ser Thr Pro Ser Glu Gly Ser Ala Pro Gly 1400 1405 1410 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu 1415 1420 1425 Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 1430 1435 1440 Glu Gly Ser Ala Pro Gly 1445 <210> 24 <211> 1445 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 24 Ala Ser His His His His His His Ser Pro Ala Gly Ser Pro Thr Ser 1 5 10 15 Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 20 25 30 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 35 40 45 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 50 55 60 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 65 70 75 80 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 85 90 95 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 100 105 110 Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 115 120 125 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 130 135 140 Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 145 150 155 160 Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 165 170 175 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu 180 185 190 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 195 200 205 Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 210 215 220 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 225 230 235 240 Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 245 250 255 Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 260 265 270 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 275 280 285 Pro Ser Glu Gly Ser Ala Pro Gly Gly Ser Ala Pro Gln Pro Ala His 290 295 300 Leu Thr Phe Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Asp Ile 305 310 315 320 Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly Asp Arg 325 330 335 Val Thr Ile Thr Cys Lys Ala Ser Gln Asp Val Ser Ile Gly Val Ala 340 345 350 Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile Tyr Ser 355 360 365 Ala Ser Tyr Arg Tyr Thr Gly Val Pro Ser Arg Phe Ser Gly Ser Gly 370 375 380 Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln Pro Glu Asp 385 390 395 400 Phe Ala Thr Tyr Tyr Cys Gln Gln Tyr Tyr Ile Tyr Pro Tyr Thr Phe 405 410 415 Gly Gln Gly Thr Lys Val Glu Ile Lys Gly Ala Thr Pro Pro Glu Thr 420 425 430 Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr Gly Gly Ser Ala Glu 435 440 445 Ser Glu Pro Pro Gly Glu Gly Glu Val Gln Leu Val Glu Ser Gly Gly 450 455 460 Gly Leu Val Gln Pro Gly Gly Ser Leu Arg Leu Ser Cys Ala Ala Ser 465 470 475 480 Gly Phe Thr Phe Thr Asp Tyr Thr Met Asp Trp Val Arg Gln Ala Pro 485 490 495 Gly Lys Gly Leu Glu Trp Val Ala Asp Val Asn Pro Asn Ser Gly Gly 500 505 510 Ser Ile Tyr Asn Gln Arg Phe Lys Gly Arg Phe Thr Leu Ser Val Asp 515 520 525 Arg Ser Lys Asn Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Ala Glu 530 535 540 Asp Thr Ala Val Tyr Cys Ala Arg Asn Leu Gly Pro Ser Phe Tyr 545 550 555 560 Phe Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 565 570 575 Gly Gly Ser Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser 580 585 590 Pro Gly Gly Thr Val Thr Leu Thr Cys Arg Ser Ser Asn Gly Ala Val 595 600 605 Thr Ser Ser Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala 610 615 620 Pro Arg Gly Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr Pro 625 630 635 640 Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu 645 650 655 Ser Gly Val Gln Pro Glu Asp Glu Ala Val Tyr Tyr Cys Ala Leu Trp 660 665 670 Tyr Pro Asn Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 675 680 685 Gly Ala Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu 690 695 700 Thr Thr Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu Val 705 710 715 720 Gln Leu Leu Glu Ser Gly Gly Gly Ile Val Gln Pro Gly Gly Ser Leu 725 730 735 Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr Ala Met 740 745 750 Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg 755 760 765 Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Ser Val 770 775 780 Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Val Tyr 785 790 795 800 Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys 805 810 815 Val Arg His Glu Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe Ala His 820 825 830 Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Thr Ala Glu Ala 835 840 845 Ala Ser Ala Ser Gly Gln Pro Ala His Leu Thr Phe Pro Pro Gly Ser 850 855 860 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala 865 870 875 880 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 885 890 895 Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr 900 905 910 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 915 920 925 Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 930 935 940 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser 945 950 955 960 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser 965 970 975 Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 980 985 990 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 995 1000 1005 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly 1010 1015 1020 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu 1025 1030 1035 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1040 1045 1050 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1055 1060 1065 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 1070 1075 1080 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1085 1090 1095 Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1100 1105 1110 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1115 1120 1125 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser 1130 1135 1140 Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr 1145 1150 1155 Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1160 1165 1170 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 1175 1180 1185 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu 1190 1195 1200 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 1205 1210 1215 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1220 1225 1230 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1235 1240 1245 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 1250 1255 1260 Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 1265 1270 1275 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1280 1285 1290 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser 1295 1300 1305 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 1310 1315 1320 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1325 1330 1335 Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1340 1345 1350 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1355 1360 1365 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly 1370 1375 1380 Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr 1385 1390 1395 Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 1400 1405 1410 Glu Ser Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1415 1420 1425 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ala Ala Glu Pro 1430 1435 1440 Glu Ala 1445 <210> 25 <211> 2024 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 25 Ala Ser Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Ser Gly Thr Ser 1 5 10 15 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 20 25 30 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 35 40 45 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 50 55 60 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Thr Pro Ala Glu Ser 65 70 75 80 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 85 90 95 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 100 105 110 Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly Thr Ser Glu Ser Ala Thr 115 120 125 Pro Glu Ser Gly Pro Gly Glu Glu Pro Ala Thr Ser Gly Ser Thr Pro 130 135 140 Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro 145 150 155 160 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro 165 170 175 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 180 185 190 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 195 200 205 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 210 215 220 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 225 230 235 240 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro 245 250 255 Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly Thr Ser Thr Glu Pro Ser 260 265 270 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 275 280 285 Pro Gly Gly Ser Ala Pro Glu Ala Gly Arg Ser Ala Asn His Thr Pro 290 295 300 Ala Gly Leu Thr Gly Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 305 310 315 320 Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 325 330 335 Asp Arg Val Thr Ile Thr Cys Arg Ala Ser Gln Asp Val Asn Thr Ala 340 345 350 Val Ala Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile 355 360 365 Tyr Ser Ala Ser Phe Leu Tyr Ser Gly Val Pro Ser Arg Phe Ser Gly 370 375 380 Ser Arg Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln Pro 385 390 395 400 Glu Asp Phe Ala Thr Tyr Tyr Cys Gln Gln His Tyr Thr Thr Pro Pro 405 410 415 Thr Phe Gly Gln Gly Thr Lys Val Glu Ile Lys Gly Ala Thr Pro Pro 420 425 430 Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr Gly Gly Ser 435 440 445 Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu Val Gln Leu Val Glu Ser 450 455 460 Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Arg Leu Ser Cys Ala 465 470 475 480 Ala Ser Gly Phe Asn Ile Lys Asp Thr Tyr Ile His Trp Val Arg Gln 485 490 495 Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Tyr Pro Thr Asn 500 505 510 Gly Tyr Thr Arg Tyr Ala Asp Ser Val Lys Gly Arg Phe Thr Ile Ser 515 520 525 Ala Asp Thr Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Ser Leu Arg 530 535 540 Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ser Arg Trp Gly Gly Asp Gly 545 550 555 560 Phe Tyr Ala Met Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 565 570 575 Ser Gly Gly Gly Ser Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr 580 585 590 Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Arg Ser Ser Asn Gly 595 600 605 Ala Val Thr Ser Ser Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly 610 615 620 Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly 625 630 635 640 Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu 645 650 655 Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Val Tyr Tyr Cys Ala 660 665 670 Leu Trp Tyr Pro Asn Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr 675 680 685 Val Leu Gly Ala Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro 690 695 700 Gly Glu Thr Thr Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly 705 710 715 720 Glu Val Gln Leu Leu Glu Ser Gly Gly Gly Ile Val Gln Pro Gly Gly 725 730 735 Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr 740 745 750 Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 755 760 765 Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp 770 775 780 Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr 785 790 795 800 Val Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr 805 810 815 Tyr Cys Val Arg His Glu Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe 820 825 830 Ala His Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Thr Ala 835 840 845 Glu Ala Ala Ser Ala Ser Gly Glu Ala Gly Arg Ser Ala Asn His Thr 850 855 860 Pro Ala Gly Leu Thr Gly Pro Ser Ala Gly Ser Pro Gly Ser Pro Ala 865 870 875 880 Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro 885 890 895 Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 900 905 910 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr 915 920 925 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 930 935 940 Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 945 950 955 960 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro 965 970 975 Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr 980 985 990 Ser Thr Glu Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 995 1000 1005 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 1010 1015 1020 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser 1025 1030 1035 Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly 1040 1045 1050 Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 1055 1060 1065 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 1070 1075 1080 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala 1085 1090 1095 Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 1100 1105 1110 Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 1115 1120 1125 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 1130 1135 1140 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala 1145 1150 1155 Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser 1160 1165 1170 Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 1175 1180 1185 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 1190 1195 1200 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro 1205 1210 1215 Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 1220 1225 1230 Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 1235 1240 1245 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 1250 1255 1260 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 1265 1270 1275 Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser 1280 1285 1290 Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 1295 1300 1305 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 1310 1315 1320 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala 1325 1330 1335 Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 1340 1345 1350 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 1355 1360 1365 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 1370 1375 1380 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser 1385 1390 1395 Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser 1400 1405 1410 Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 1415 1420 1425 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 1430 1435 1440 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala 1445 1450 1455 Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 1460 1465 1470 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 1475 1480 1485 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 1490 1495 1500 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro 1505 1510 1515 Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser 1520 1525 1530 Thr Glu Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 1535 1540 1545 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 1550 1555 1560 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser 1565 1570 1575 Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser 1580 1585 1590 Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 1595 1600 1605 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 1610 1615 1620 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala 1625 1630 1635 Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 1640 1645 1650 Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 1655 1660 1665 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 1670 1675 1680 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 1685 1690 1695 Ser Glu Gly Ser Ala Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 1700 1705 1710 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 1715 1720 1725 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 1730 1735 1740 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala 1745 1750 1755 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 1760 1765 1770 Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 1775 1780 1785 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 1790 1795 1800 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala 1805 1810 1815 Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 1820 1825 1830 Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Thr Glu Thr 1835 1840 1845 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr 1850 1855 1860 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu 1865 1870 1875 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 1880 1885 1890 Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 1895 1900 1905 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1910 1915 1920 Ala Thr Glu Ser Pro Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 1925 1930 1935 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu 1940 1945 1950 Gly Ser Ala Pro Gly Thr Ser Ala Glu Ser Ala Thr Pro Glu Ser 1955 1960 1965 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly 1970 1975 1980 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 1985 1990 1995 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 2000 2005 2010Pro Glu Ser Gly Pro Gly Thr Glu Ser Ala Ser 2015 2020 <210> 26 <211> 1461 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 26 Ala Ser His His His His His His Ser Pro Ala Gly Ser Pro Thr Ser 1 5 10 15 Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 20 25 30 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 35 40 45 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 50 55 60 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 65 70 75 80 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 85 90 95 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 100 105 110 Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 115 120 125 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 130 135 140 Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 145 150 155 160 Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 165 170 175 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu 180 185 190 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 195 200 205 Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 210 215 220 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 225 230 235 240 Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 245 250 255 Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 260 265 270 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 275 280 285 Pro Ser Glu Gly Ser Ala Pro Gly Gly Ser Ala Pro Glu Ala Gly Ser 290 295 300 Pro Gly Lys Asp Gly Val Arg Gly Leu Thr Gly Pro Ala Thr Ser Gly 305 310 315 320 Ser Glu Thr Pro Gly Thr Asp Ile Gln Met Thr Gln Ser Pro Ser Ser 325 330 335 Leu Ser Ala Ser Val Gly Asp Arg Val Thr Ile Thr Cys Lys Ala Ser 340 345 350 Gln Asp Val Ser Ile Gly Val Ala Trp Tyr Gln Gln Lys Pro Gly Lys 355 360 365 Ala Pro Lys Leu Leu Ile Tyr Ser Ala Ser Tyr Arg Tyr Thr Gly Val 370 375 380 Pro Ser Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr 385 390 395 400 Ile Ser Ser Leu Gln Pro Glu Asp Phe Ala Thr Tyr Tyr Cys Gln Gln 405 410 415 Tyr Tyr Ile Tyr Pro Tyr Thr Phe Gly Gln Gly Thr Lys Val Glu Ile 420 425 430 Lys Gly Ala Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly 435 440 445 Glu Thr Thr Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu 450 455 460 Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser 465 470 475 480 Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Thr Asp Tyr Thr 485 490 495 Met Asp Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala 500 505 510 Asp Val Asn Pro Asn Ser Gly Gly Ser Ile Tyr Asn Gln Arg Phe Lys 515 520 525 Gly Arg Phe Thr Leu Ser Val Asp Arg Ser Lys Asn Thr Leu Tyr Leu 530 535 540 Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala 545 550 555 560 Arg Asn Leu Gly Pro Ser Phe Tyr Phe Asp Tyr Trp Gly Gln Gly Thr 565 570 575 Leu Val Thr Val Ser Ser Gly Gly Gly Gly Ser Glu Leu Val Val Thr 580 585 590 Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr 595 600 605 Cys Arg Ser Ser Asn Gly Ala Val Thr Ser Ser Asn Tyr Ala Asn Trp 610 615 620 Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr 625 630 635 640 Asn Lys Arg Ala Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu 645 650 655 Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu 660 665 670 Ala Val Tyr Tyr Cys Ala Leu Trp Tyr Pro Asn Leu Trp Val Phe Gly 675 680 685 Gly Gly Thr Lys Leu Thr Val Leu Gly Ala Thr Pro Pro Glu Thr Gly 690 695 700 Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr Gly Gly Ser Ala Glu Ser 705 710 715 720 Glu Pro Pro Gly Glu Gly Glu Val Gln Leu Leu Glu Ser Gly Gly Gly 725 730 735 Ile Val Gln Pro Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly 740 745 750 Phe Thr Phe Asn Thr Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly 755 760 765 Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr 770 775 780 Ala Thr Tyr Tyr Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg 785 790 795 800 Asp Asp Ser Lys Asn Thr Val Tyr Leu Gln Met Asn Asn Leu Lys Thr 805 810 815 Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His Glu Asn Phe Gly Asn 820 825 830 Ser Tyr Val Ser Trp Phe Ala His Trp Gly Gln Gly Thr Leu Val Thr 835 840 845 Val Ser Ser Gly Thr Ala Glu Ala Ala Ser Ala Ser Gly Glu Ala Gly 850 855 860 Ser Pro Gly Lys Asp Gly Val Arg Gly Leu Thr Gly Pro Pro Gly Ser 865 870 875 880 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala 885 890 895 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 900 905 910 Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr 915 920 925 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 930 935 940 Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 945 950 955 960 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser 965 970 975 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser 980 985 990 Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 995 1000 1005 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 1010 1015 1020 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala 1025 1030 1035 Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 1040 1045 1050 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 1055 1060 1065 Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 1070 1075 1080 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu 1085 1090 1095 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 1100 1105 1110 Gly Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 1115 1120 1125 Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 1130 1135 1140 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu 1145 1150 1155 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro 1160 1165 1170 Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 1175 1180 1185 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly 1190 1195 1200 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr 1205 1210 1215 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 1220 1225 1230 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 1235 1240 1245 Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 1250 1255 1260 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 1265 1270 1275 Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 1280 1285 1290 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 1295 1300 1305 Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 1310 1315 1320 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu 1325 1330 1335 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 1340 1345 1350 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 1355 1360 1365 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 1370 1375 1380 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala 1385 1390 1395 Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro 1400 1405 1410 Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr 1415 1420 1425 Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 1430 1435 1440 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ala Ala Glu 1445 1450 1455 Pro Glu Ala 1460 <210> 27 <211> 1452 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 27 Ala Ser Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Ser Gly Thr Ser 1 5 10 15 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 20 25 30 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 35 40 45 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 50 55 60 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Thr Pro Ala Glu Ser 65 70 75 80 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 85 90 95 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 100 105 110 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 115 120 125 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 130 135 140 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro 145 150 155 160 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro 165 170 175 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 180 185 190 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 195 200 205 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 210 215 220 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 225 230 235 240 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro 245 250 255 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 260 265 270 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 275 280 285 Pro Gly Gly Ser Ala Pro Arg Thr Gly Arg Thr Gly Glu Ser Ala Asn 290 295 300 Glu Thr Pro Ala Gly Leu Gly Gly Pro Ala Thr Ser Gly Ser Glu Thr 305 310 315 320 Pro Gly Thr Glu Ile Val Leu Thr Gln Ser Pro Ala Thr Leu Ser Leu 325 330 335 Ser Pro Gly Glu Arg Ala Thr Leu Ser Cys Lys Ala Ser Gln Asp Val 340 345 350 Ser Ile Gly Val Ala Trp Tyr Gln Gln Lys Pro Gly Gln Ala Pro Arg 355 360 365 Leu Leu Ile Tyr Ser Ala Ser Tyr Arg Tyr Ser Gly Val Pro Ala Arg 370 375 380 Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser 385 390 395 400 Leu Glu Pro Glu Asp Phe Ala Val Tyr Tyr Cys Gln Gln Tyr Tyr Ile 405 410 415 Tyr Pro Tyr Thr Phe Gly Gln Gly Thr Lys Val Glu Ile Lys Gly Ala 420 425 430 Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr 435 440 445 Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Gln Val Gln Leu 450 455 460 Val Gln Ser Gly Val Glu Val Lys Lys Pro Gly Ala Ser Val Lys Val 465 470 475 480 Ser Cys Lys Ala Ser Gly Phe Thr Phe Thr Asp Tyr Thr Met Asp Trp 485 490 495 Val Arg Gln Ala Pro Gly Gln Gly Leu Glu Trp Met Ala Asp Val Asn 500 505 510 Pro Asn Ser Gly Gly Ser Ile Tyr Asn Gln Arg Phe Lys Gly Arg Val 515 520 525 Thr Leu Thr Thr Asp Ser Ser Thr Thr Thr Thr Ala Tyr Met Glu Leu Lys 530 535 540 Ser Leu Gln Phe Asp Asp Thr Ala Val Tyr Tyr Cys Ala Arg Asn Leu 545 550 555 560 Gly Pro Ser Phe Tyr Phe Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr 565 570 575 Val Ser Ser Gly Gly Gly Ser Glu Leu Val Val Thr Gln Glu Pro Ser 580 585 590 Leu Thr Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Arg Ser Ser 595 600 605 Asn Gly Ala Val Thr Ser Ser Asn Tyr Ala Asn Trp Val Gln Gln Lys 610 615 620 Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Asn Lys Arg Ala 625 630 635 640 Pro Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala 645 650 655 Ala Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Val Tyr Tyr 660 665 670 Cys Ala Leu Trp Tyr Pro Asn Leu Trp Val Phe Gly Gly Gly Thr Lys 675 680 685 Leu Thr Val Leu Gly Ala Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu 690 695 700 Ser Pro Gly Glu Thr Thr Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly 705 710 715 720 Glu Gly Glu Val Gln Leu Leu Glu Ser Gly Gly Gly Ile Val Gln Pro 725 730 735 Gly Gly Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn 740 745 750 Thr Tyr Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu 755 760 765 Trp Val Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr 770 775 780 Ala Asp Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys 785 790 795 800 Asn Thr Val Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala 805 810 815 Val Tyr Tyr Cys Val Arg His Glu Asn Phe Gly Asn Ser Tyr Val Ser 820 825 830 Trp Phe Ala His Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly 835 840 845 Thr Ala Glu Ala Ala Ser Ala Ser Gly Arg Thr Gly Arg Thr Gly Glu 850 855 860 Ser Ala Asn Glu Thr Pro Ala Gly Leu Gly Gly Pro Gly Ser Glu Thr 865 870 875 880 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 885 890 895 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 900 905 910 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 915 920 925 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 930 935 940 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 945 950 955 960 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 965 970 975 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 980 985 990 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 995 1000 1005 Gly Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 1010 1015 1020 Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 1025 1030 1035 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu 1040 1045 1050 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro 1055 1060 1065 Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 1070 1075 1080 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly 1085 1090 1095 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr 1100 1105 1110 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 1115 1120 1125 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 1130 1135 1140 Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 1145 1150 1155 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 1160 1165 1170 Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 1175 1180 1185 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 1190 1195 1200 Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 1205 1210 1215 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu 1220 1225 1230 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 1235 1240 1245 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 1250 1255 1260 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 1265 1270 1275 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala 1280 1285 1290 Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro 1295 1300 1305 Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr 1310 1315 1320 Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 1325 1330 1335 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu 1340 1345 1350 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 1355 1360 1365 Gly Ser Thr Glu Thr Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 1370 1375 1380 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly 1385 1390 1395 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr 1400 1405 1410 Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 1415 1420 1425 Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 1430 1435 1440 Gly Pro Gly Ser Glu Pro Ala Thr Ser 1445 1450 <210> 28 <211> 1445 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 28 Ala Ser His His His His His His Ser Pro Ala Gly Ser Pro Thr Ser 1 5 10 15 Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 20 25 30 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 35 40 45 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 50 55 60 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 65 70 75 80 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 85 90 95 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 100 105 110 Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 115 120 125 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 130 135 140 Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 145 150 155 160 Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 165 170 175 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu 180 185 190 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 195 200 205 Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 210 215 220 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 225 230 235 240 Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 245 250 255 Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 260 265 270 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 275 280 285 Pro Ser Glu Gly Ser Ala Pro Gly Gly Ser Ala Pro Ser Pro Glu Ala 290 295 300 Gln Ala Ala Ala Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Asp Ile 305 310 315 320 Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly Asp Arg 325 330 335 Val Thr Ile Thr Cys Lys Ala Ser Gln Asp Val Ser Ile Gly Val Ala 340 345 350 Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile Tyr Ser 355 360 365 Ala Ser Tyr Arg Tyr Thr Gly Val Pro Ser Arg Phe Ser Gly Ser Gly 370 375 380 Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln Pro Glu Asp 385 390 395 400 Phe Ala Thr Tyr Tyr Cys Gln Gln Tyr Tyr Ile Tyr Pro Tyr Thr Phe 405 410 415 Gly Gln Gly Thr Lys Val Glu Ile Lys Gly Ala Thr Pro Pro Glu Thr 420 425 430 Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr Gly Gly Ser Ala Glu 435 440 445 Ser Glu Pro Pro Gly Glu Gly Glu Val Gln Leu Val Glu Ser Gly Gly 450 455 460 Gly Leu Val Gln Pro Gly Gly Ser Leu Arg Leu Ser Cys Ala Ala Ser 465 470 475 480 Gly Phe Thr Phe Thr Asp Tyr Thr Met Asp Trp Val Arg Gln Ala Pro 485 490 495 Gly Lys Gly Leu Glu Trp Val Ala Asp Val Asn Pro Asn Ser Gly Gly 500 505 510 Ser Ile Tyr Asn Gln Arg Phe Lys Gly Arg Phe Thr Leu Ser Val Asp 515 520 525 Arg Ser Lys Asn Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Ala Glu 530 535 540 Asp Thr Ala Val Tyr Cys Ala Arg Asn Leu Gly Pro Ser Phe Tyr 545 550 555 560 Phe Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 565 570 575 Gly Gly Ser Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser 580 585 590 Pro Gly Gly Thr Val Thr Leu Thr Cys Arg Ser Ser Asn Gly Ala Val 595 600 605 Thr Ser Ser Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala 610 615 620 Pro Arg Gly Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr Pro 625 630 635 640 Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu 645 650 655 Ser Gly Val Gln Pro Glu Asp Glu Ala Val Tyr Tyr Cys Ala Leu Trp 660 665 670 Tyr Pro Asn Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 675 680 685 Gly Ala Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu 690 695 700 Thr Thr Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu Val 705 710 715 720 Gln Leu Leu Glu Ser Gly Gly Gly Ile Val Gln Pro Gly Gly Ser Leu 725 730 735 Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr Ala Met 740 745 750 Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg 755 760 765 Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Ser Val 770 775 780 Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Val Tyr 785 790 795 800 Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys 805 810 815 Val Arg His Glu Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe Ala His 820 825 830 Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Thr Ala Glu Ala 835 840 845 Ala Ser Ala Ser Gly Ser Pro Glu Ala Gln Ala Ala Ala Pro Gly Ser 850 855 860 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala 865 870 875 880 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 885 890 895 Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr 900 905 910 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 915 920 925 Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 930 935 940 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser 945 950 955 960 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser 965 970 975 Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 980 985 990 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 995 1000 1005 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly 1010 1015 1020 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu 1025 1030 1035 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1040 1045 1050 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1055 1060 1065 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 1070 1075 1080 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1085 1090 1095 Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1100 1105 1110 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1115 1120 1125 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser 1130 1135 1140 Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr 1145 1150 1155 Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1160 1165 1170 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 1175 1180 1185 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu 1190 1195 1200 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 1205 1210 1215 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1220 1225 1230 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1235 1240 1245 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 1250 1255 1260 Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 1265 1270 1275 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1280 1285 1290 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser 1295 1300 1305 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 1310 1315 1320 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1325 1330 1335 Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1340 1345 1350 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1355 1360 1365 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly 1370 1375 1380 Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr 1385 1390 1395 Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 1400 1405 1410 Glu Ser Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1415 1420 1425 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ala Ala Glu Pro 1430 1435 1440 Glu Ala 1445 <210> 29 <211> 1445 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 29 Ala Ser His His His His His His Ser Pro Ala Gly Ser Pro Thr Ser 1 5 10 15 Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 20 25 30 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 35 40 45 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 50 55 60 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 65 70 75 80 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 85 90 95 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 100 105 110 Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 115 120 125 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 130 135 140 Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 145 150 155 160 Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 165 170 175 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu 180 185 190 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 195 200 205 Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 210 215 220 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 225 230 235 240 Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 245 250 255 Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 260 265 270 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 275 280 285 Pro Ser Glu Gly Ser Ala Pro Gly Gly Ser Ala Pro Leu Thr Ser Asp 290 295 300 Leu Gln Ala Gln Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Asp Ile 305 310 315 320 Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly Asp Arg 325 330 335 Val Thr Ile Thr Cys Gln Ala Ser Gln Asp Ile Ser Asn Tyr Leu Asn 340 345 350 Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile Tyr Asp 355 360 365 Ala Ser Asn Leu Glu Thr Gly Val Pro Ser Arg Phe Ser Gly Ser Gly 370 375 380 Ser Gly Thr Asp Phe Thr Phe Thr Ile Ser Ser Leu Gln Pro Glu Asp 385 390 395 400 Ile Ala Thr Tyr Phe Cys Gln His Phe Asp His Leu Pro Leu Ala Phe 405 410 415 Gly Gly Gly Thr Lys Val Glu Ile Lys Gly Ala Thr Pro Pro Glu Thr 420 425 430 Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr Gly Gly Ser Ala Glu 435 440 445 Ser Glu Pro Pro Gly Glu Gly Gln Val Gln Leu Gln Glu Ser Gly Pro 450 455 460 Gly Leu Val Lys Pro Ser Glu Thr Leu Ser Leu Thr Cys Thr Val Ser 465 470 475 480 Gly Gly Ser Val Ser Ser Gly Asp Tyr Tyr Trp Thr Trp Ile Arg Gln 485 490 495 Ser Pro Gly Lys Gly Leu Glu Trp Ile Gly His Ile Tyr Tyr Ser Gly 500 505 510 Asn Thr Asn Tyr Asn Pro Ser Leu Lys Ser Arg Leu Thr Ile Ser Ile 515 520 525 Asp Thr Ser Lys Thr Gln Phe Ser Leu Lys Leu Ser Ser Val Thr Ala 530 535 540 Ala Asp Thr Ala Ile Tyr Tyr Cys Val Arg Asp Arg Val Thr Gly Ala 545 550 555 560 Phe Asp Ile Trp Gly Gln Gly Thr Met Val Thr Val Ser Ser Gly Gly 565 570 575 Gly Gly Ser Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser 580 585 590 Pro Gly Gly Thr Val Thr Leu Thr Cys Arg Ser Ser Thr Gly Ala Val 595 600 605 Thr Thr Ser Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala 610 615 620 Pro Arg Gly Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr Pro 625 630 635 640 Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu 645 650 655 Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Ala Leu Trp 660 665 670 Tyr Ser Asn Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 675 680 685 Gly Ala Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu 690 695 700 Thr Thr Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu Val 705 710 715 720 Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 725 730 735 Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr Ala Met 740 745 750 Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg 755 760 765 Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Ser Val 770 775 780 Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr 785 790 795 800 Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys 805 810 815 Val Arg His Gly Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe Ala Tyr 820 825 830 Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Thr Ala Glu Ala 835 840 845 Ala Ser Ala Ser Gly Leu Thr Ser Asp Leu Gln Ala Gln Pro Gly Ser 850 855 860 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala 865 870 875 880 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 885 890 895 Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr 900 905 910 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 915 920 925 Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 930 935 940 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser 945 950 955 960 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser 965 970 975 Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 980 985 990 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 995 1000 1005 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly 1010 1015 1020 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu 1025 1030 1035 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1040 1045 1050 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1055 1060 1065 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 1070 1075 1080 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1085 1090 1095 Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1100 1105 1110 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1115 1120 1125 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser 1130 1135 1140 Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr 1145 1150 1155 Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1160 1165 1170 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 1175 1180 1185 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu 1190 1195 1200 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 1205 1210 1215 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1220 1225 1230 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1235 1240 1245 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 1250 1255 1260 Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 1265 1270 1275 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1280 1285 1290 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser 1295 1300 1305 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 1310 1315 1320 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1325 1330 1335 Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1340 1345 1350 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1355 1360 1365 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly 1370 1375 1380 Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr 1385 1390 1395 Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 1400 1405 1410 Glu Ser Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1415 1420 1425 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ala Ala Glu Pro 1430 1435 1440 Glu Ala 1445 <210> 30 <211> 1445 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 30 Ala Ser His His His His His His Ser Pro Ala Gly Ser Pro Thr Ser 1 5 10 15 Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 20 25 30 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 35 40 45 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 50 55 60 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 65 70 75 80 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 85 90 95 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 100 105 110 Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 115 120 125 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 130 135 140 Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 145 150 155 160 Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 165 170 175 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu 180 185 190 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 195 200 205 Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 210 215 220 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 225 230 235 240 Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 245 250 255 Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 260 265 270 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 275 280 285 Pro Ser Glu Gly Ser Ala Pro Gly Gly Ser Ala Pro Gln Pro Ala His 290 295 300 Leu Thr Phe Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Asp Ile 305 310 315 320 Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly Asp Arg 325 330 335 Val Thr Ile Thr Cys Gln Ala Ser Gln Asp Ile Ser Asn Tyr Leu Asn 340 345 350 Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile Tyr Asp 355 360 365 Ala Ser Asn Leu Glu Thr Gly Val Pro Ser Arg Phe Ser Gly Ser Gly 370 375 380 Ser Gly Thr Asp Phe Thr Phe Thr Ile Ser Ser Leu Gln Pro Glu Asp 385 390 395 400 Ile Ala Thr Tyr Phe Cys Gln His Phe Asp His Leu Pro Leu Ala Phe 405 410 415 Gly Gly Gly Thr Lys Val Glu Ile Lys Gly Ala Thr Pro Pro Glu Thr 420 425 430 Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr Gly Gly Ser Ala Glu 435 440 445 Ser Glu Pro Pro Gly Glu Gly Gln Val Gln Leu Gln Glu Ser Gly Pro 450 455 460 Gly Leu Val Lys Pro Ser Glu Thr Leu Ser Leu Thr Cys Thr Val Ser 465 470 475 480 Gly Gly Ser Val Ser Ser Gly Asp Tyr Tyr Trp Thr Trp Ile Arg Gln 485 490 495 Ser Pro Gly Lys Gly Leu Glu Trp Ile Gly His Ile Tyr Tyr Ser Gly 500 505 510 Asn Thr Asn Tyr Asn Pro Ser Leu Lys Ser Arg Leu Thr Ile Ser Ile 515 520 525 Asp Thr Ser Lys Thr Gln Phe Ser Leu Lys Leu Ser Ser Val Thr Ala 530 535 540 Ala Asp Thr Ala Ile Tyr Tyr Cys Val Arg Asp Arg Val Thr Gly Ala 545 550 555 560 Phe Asp Ile Trp Gly Gln Gly Thr Met Val Thr Val Ser Ser Gly Gly 565 570 575 Gly Gly Ser Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser 580 585 590 Pro Gly Gly Thr Val Thr Leu Thr Cys Arg Ser Ser Thr Gly Ala Val 595 600 605 Thr Thr Ser Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala 610 615 620 Pro Arg Gly Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr Pro 625 630 635 640 Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu 645 650 655 Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Ala Leu Trp 660 665 670 Tyr Ser Asn Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 675 680 685 Gly Ala Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu 690 695 700 Thr Thr Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu Val 705 710 715 720 Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 725 730 735 Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr Ala Met 740 745 750 Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg 755 760 765 Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Ser Val 770 775 780 Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr 785 790 795 800 Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys 805 810 815 Val Arg His Gly Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe Ala Tyr 820 825 830 Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Thr Ala Glu Ala 835 840 845 Ala Ser Ala Ser Gly Gln Pro Ala His Leu Thr Phe Pro Pro Gly Ser 850 855 860 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala 865 870 875 880 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 885 890 895 Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr 900 905 910 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 915 920 925 Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 930 935 940 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser 945 950 955 960 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser 965 970 975 Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 980 985 990 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 995 1000 1005 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly 1010 1015 1020 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu 1025 1030 1035 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1040 1045 1050 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1055 1060 1065 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 1070 1075 1080 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1085 1090 1095 Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1100 1105 1110 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1115 1120 1125 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser 1130 1135 1140 Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr 1145 1150 1155 Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1160 1165 1170 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 1175 1180 1185 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu 1190 1195 1200 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 1205 1210 1215 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1220 1225 1230 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1235 1240 1245 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 1250 1255 1260 Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 1265 1270 1275 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1280 1285 1290 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser 1295 1300 1305 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 1310 1315 1320 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1325 1330 1335 Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1340 1345 1350 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1355 1360 1365 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly 1370 1375 1380 Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr 1385 1390 1395 Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 1400 1405 1410 Glu Ser Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1415 1420 1425 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ala Ala Glu Pro 1430 1435 1440 Glu Ala 1445 <210> 31 <211> 1745 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 31 Ala Ser Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Ser Gly Thr Ser 1 5 10 15 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 20 25 30 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 35 40 45 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 50 55 60 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Thr Pro Ala Glu Ser 65 70 75 80 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 85 90 95 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 100 105 110 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 115 120 125 Pro Glu Ser Gly Pro Gly Glu Glu Pro Ala Thr Ser Gly Ser Thr Pro 130 135 140 Glu Ser Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro 145 150 155 160 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro 165 170 175 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 180 185 190 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 195 200 205 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 210 215 220 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 225 230 235 240 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro 245 250 255 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 260 265 270 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 275 280 285 Pro Gly Gly Ser Ala Pro Gly Ala Gly Arg Thr Asp Asn His Glu Pro 290 295 300 Leu Glu Leu Gly Ala Ala Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 305 310 315 320 Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 325 330 335 Asp Arg Val Thr Ile Thr Cys Arg Ala Ser Gln Asp Val Asn Thr Ala 340 345 350 Val Ala Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile 355 360 365 Tyr Ser Ala Ser Phe Leu Tyr Ser Gly Val Pro Ser Arg Phe Ser Gly 370 375 380 Ser Arg Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln Pro 385 390 395 400 Glu Asp Phe Ala Thr Tyr Tyr Cys Gln Gln His Tyr Thr Thr Pro Pro 405 410 415 Thr Phe Gly Gln Gly Thr Lys Val Glu Ile Lys Gly Ala Thr Pro Pro 420 425 430 Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr Gly Gly Ser 435 440 445 Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu Val Gln Leu Val Glu Ser 450 455 460 Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Arg Leu Ser Cys Ala 465 470 475 480 Ala Ser Gly Phe Asn Ile Lys Asp Thr Tyr Ile His Trp Val Arg Gln 485 490 495 Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Tyr Pro Thr Asn 500 505 510 Gly Tyr Thr Arg Tyr Ala Asp Ser Val Lys Gly Arg Phe Thr Ile Ser 515 520 525 Ala Asp Thr Ser Lys Asn Thr Ala Tyr Leu Gln Met Asn Ser Leu Arg 530 535 540 Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ser Arg Trp Gly Gly Asp Gly 545 550 555 560 Phe Tyr Ala Met Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser 565 570 575 Ser Gly Gly Gly Ser Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr 580 585 590 Val Ser Pro Gly Gly Thr Val Thr Leu Thr Cys Arg Ser Ser Thr Gly 595 600 605 Ala Val Thr Thr Ser Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly 610 615 620 Gln Ala Pro Arg Gly Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly 625 630 635 640 Thr Pro Ala Arg Phe Ser Gly Ser Ser Leu Gly Gly Ser Ala Ala Leu 645 650 655 Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Ala 660 665 670 Leu Trp Tyr Ser Asn Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr 675 680 685 Val Leu Gly Ala Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro 690 695 700 Gly Glu Thr Thr Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly 705 710 715 720 Glu Val Gln Leu Gln Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 725 730 735 Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr 740 745 750 Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 755 760 765 Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp 770 775 780 Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr 785 790 795 800 Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr 805 810 815 Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe 820 825 830 Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Thr Ala 835 840 845 Glu Ala Ala Ser Ala Ser Gly Gly Ala Gly Arg Thr Asp Asn His Glu 850 855 860 Pro Leu Glu Leu Gly Ala Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 865 870 875 880 Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 885 890 895 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala 900 905 910 Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu 915 920 925 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 930 935 940 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro 945 950 955 960 Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly 965 970 975 Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 980 985 990 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr 995 1000 1005 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 1010 1015 1020 Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr 1025 1030 1035 Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 1040 1045 1050 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu 1055 1060 1065 Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 1070 1075 1080 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 1085 1090 1095 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly 1100 1105 1110 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 1115 1120 1125 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 1130 1135 1140 Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 1145 1150 1155 Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly 1160 1165 1170 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro 1175 1180 1185 Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 1190 1195 1200 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 1205 1210 1215 Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 1220 1225 1230 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 1235 1240 1245 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 1250 1255 1260 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 1265 1270 1275 Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 1280 1285 1290 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu 1295 1300 1305 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 1310 1315 1320 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 1325 1330 1335 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly 1340 1345 1350 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr 1355 1360 1365 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 1370 1375 1380 Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr 1385 1390 1395 Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 1400 1405 1410 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu 1415 1420 1425 Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 1430 1435 1440 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 1445 1450 1455 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly 1460 1465 1470 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro 1475 1480 1485 Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 1490 1495 1500 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 1505 1510 1515 Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 1520 1525 1530 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro 1535 1540 1545 Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 1550 1555 1560 Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr 1565 1570 1575 Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 1580 1585 1590 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu 1595 1600 1605 Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 1610 1615 1620 Pro Glu Ser Gly Pro Gly Phe Thr Ala Asx Thr Ser Glu Ser Ala 1625 1630 1635 Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Pro 1640 1645 1650 Thr Glu Ser Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 1655 1660 1665 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 1670 1675 1680 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Glu Ser Thr Pro 1685 1690 1695 Ser Glu Gly Ser Ala Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 1700 1705 1710 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 1715 1720 1725 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Glu Pro 1730 1735 1740 Glu Ala 1745 <210> 32 <211> 1445 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 32 Ala Ser His His His His His His Ser Pro Ala Gly Ser Pro Thr Ser 1 5 10 15 Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 20 25 30 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 35 40 45 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 50 55 60 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 65 70 75 80 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 85 90 95 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 100 105 110 Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 115 120 125 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 130 135 140 Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 145 150 155 160 Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 165 170 175 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu 180 185 190 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 195 200 205 Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 210 215 220 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 225 230 235 240 Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 245 250 255 Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 260 265 270 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 275 280 285 Pro Ser Glu Gly Ser Ala Pro Gly Gly Ser Ala Pro Gln Pro Val Ser 290 295 300 Leu Ala Asn Thr Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Asp Ile 305 310 315 320 Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly Asp Arg 325 330 335 Val Thr Ile Thr Cys Gln Ala Ser Gln Asp Ile Ser Asn Tyr Leu Asn 340 345 350 Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile Tyr Asp 355 360 365 Ala Ser Asn Leu Glu Thr Gly Val Pro Ser Arg Phe Ser Gly Ser Gly 370 375 380 Ser Gly Thr Asp Phe Thr Phe Thr Ile Ser Ser Leu Gln Pro Glu Asp 385 390 395 400 Ile Ala Thr Tyr Phe Cys Gln His Phe Asp His Leu Pro Leu Ala Phe 405 410 415 Gly Gly Gly Thr Lys Val Glu Ile Lys Gly Ala Thr Pro Pro Glu Thr 420 425 430 Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr Gly Gly Ser Ala Glu 435 440 445 Ser Glu Pro Pro Gly Glu Gly Gln Val Gln Leu Gln Glu Ser Gly Pro 450 455 460 Gly Leu Val Lys Pro Ser Glu Thr Leu Ser Leu Thr Cys Thr Val Ser 465 470 475 480 Gly Gly Ser Val Ser Ser Gly Asp Tyr Tyr Trp Thr Trp Ile Arg Gln 485 490 495 Ser Pro Gly Lys Gly Leu Glu Trp Ile Gly His Ile Tyr Tyr Ser Gly 500 505 510 Asn Thr Asn Tyr Asn Pro Ser Leu Lys Ser Arg Leu Thr Ile Ser Ile 515 520 525 Asp Thr Ser Lys Thr Gln Phe Ser Leu Lys Leu Ser Ser Val Thr Ala 530 535 540 Ala Asp Thr Ala Ile Tyr Tyr Cys Val Arg Asp Arg Val Thr Gly Ala 545 550 555 560 Phe Asp Ile Trp Gly Gln Gly Thr Met Val Thr Val Ser Ser Gly Gly 565 570 575 Gly Gly Ser Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser 580 585 590 Pro Gly Gly Thr Val Thr Leu Thr Cys Arg Ser Ser Thr Gly Ala Val 595 600 605 Thr Thr Ser Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala 610 615 620 Pro Arg Gly Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr Pro 625 630 635 640 Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu 645 650 655 Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Ala Leu Trp 660 665 670 Tyr Ser Asn Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 675 680 685 Gly Ala Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu 690 695 700 Thr Thr Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu Val 705 710 715 720 Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 725 730 735 Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr Ala Met 740 745 750 Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg 755 760 765 Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Ser Val 770 775 780 Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr 785 790 795 800 Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys 805 810 815 Val Arg His Gly Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe Ala Tyr 820 825 830 Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Thr Ala Glu Ala 835 840 845 Ala Ser Ala Ser Gly Gln Pro Val Ser Leu Ala Asn Thr Pro Gly Ser 850 855 860 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala 865 870 875 880 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 885 890 895 Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr 900 905 910 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 915 920 925 Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 930 935 940 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser 945 950 955 960 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser 965 970 975 Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 980 985 990 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 995 1000 1005 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly 1010 1015 1020 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu 1025 1030 1035 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1040 1045 1050 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1055 1060 1065 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 1070 1075 1080 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1085 1090 1095 Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1100 1105 1110 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1115 1120 1125 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser 1130 1135 1140 Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr 1145 1150 1155 Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1160 1165 1170 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 1175 1180 1185 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu 1190 1195 1200 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 1205 1210 1215 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1220 1225 1230 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1235 1240 1245 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 1250 1255 1260 Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 1265 1270 1275 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1280 1285 1290 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser 1295 1300 1305 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 1310 1315 1320 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1325 1330 1335 Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1340 1345 1350 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1355 1360 1365 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly 1370 1375 1380 Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr 1385 1390 1395 Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 1400 1405 1410 Glu Ser Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1415 1420 1425 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ala Ala Glu Pro 1430 1435 1440 Glu Ala 1445 <210> 33 <211> 1445 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 33 Ala Ser His His His His His His Ser Pro Ala Gly Ser Pro Thr Ser 1 5 10 15 Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 20 25 30 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 35 40 45 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 50 55 60 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 65 70 75 80 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 85 90 95 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 100 105 110 Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 115 120 125 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 130 135 140 Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 145 150 155 160 Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 165 170 175 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu 180 185 190 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 195 200 205 Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 210 215 220 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 225 230 235 240 Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 245 250 255 Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 260 265 270 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 275 280 285 Pro Ser Glu Gly Ser Ala Pro Gly Gly Ser Ala Pro Gly Pro Ser Gly 290 295 300 His Met Gly Arg Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Asp Ile 305 310 315 320 Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly Asp Arg 325 330 335 Val Thr Ile Thr Cys Gln Ala Ser Gln Asp Ile Ser Asn Tyr Leu Asn 340 345 350 Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile Tyr Asp 355 360 365 Ala Ser Asn Leu Glu Thr Gly Val Pro Ser Arg Phe Ser Gly Ser Gly 370 375 380 Ser Gly Thr Asp Phe Thr Phe Thr Ile Ser Ser Leu Gln Pro Glu Asp 385 390 395 400 Ile Ala Thr Tyr Phe Cys Gln His Phe Asp His Leu Pro Leu Ala Phe 405 410 415 Gly Gly Gly Thr Lys Val Glu Ile Lys Gly Ala Thr Pro Pro Glu Thr 420 425 430 Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr Gly Gly Ser Ala Glu 435 440 445 Ser Glu Pro Pro Gly Glu Gly Gln Val Gln Leu Gln Glu Ser Gly Pro 450 455 460 Gly Leu Val Lys Pro Ser Glu Thr Leu Ser Leu Thr Cys Thr Val Ser 465 470 475 480 Gly Gly Ser Val Ser Ser Gly Asp Tyr Tyr Trp Thr Trp Ile Arg Gln 485 490 495 Ser Pro Gly Lys Gly Leu Glu Trp Ile Gly His Ile Tyr Tyr Ser Gly 500 505 510 Asn Thr Asn Tyr Asn Pro Ser Leu Lys Ser Arg Leu Thr Ile Ser Ile 515 520 525 Asp Thr Ser Lys Thr Gln Phe Ser Leu Lys Leu Ser Ser Val Thr Ala 530 535 540 Ala Asp Thr Ala Ile Tyr Tyr Cys Val Arg Asp Arg Val Thr Gly Ala 545 550 555 560 Phe Asp Ile Trp Gly Gln Gly Thr Met Val Thr Val Ser Ser Gly Gly 565 570 575 Gly Gly Ser Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser 580 585 590 Pro Gly Gly Thr Val Thr Leu Thr Cys Arg Ser Ser Thr Gly Ala Val 595 600 605 Thr Thr Ser Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala 610 615 620 Pro Arg Gly Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr Pro 625 630 635 640 Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu 645 650 655 Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Ala Leu Trp 660 665 670 Tyr Ser Asn Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 675 680 685 Gly Ala Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu 690 695 700 Thr Thr Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu Val 705 710 715 720 Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 725 730 735 Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr Ala Met 740 745 750 Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg 755 760 765 Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Ser Val 770 775 780 Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr 785 790 795 800 Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys 805 810 815 Val Arg His Gly Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe Ala Tyr 820 825 830 Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Thr Ala Glu Ala 835 840 845 Ala Ser Ala Ser Gly Gly Pro Ser Gly His Met Gly Arg Pro Gly Ser 850 855 860 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala 865 870 875 880 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 885 890 895 Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr 900 905 910 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 915 920 925 Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 930 935 940 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser 945 950 955 960 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser 965 970 975 Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 980 985 990 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 995 1000 1005 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly 1010 1015 1020 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu 1025 1030 1035 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1040 1045 1050 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1055 1060 1065 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 1070 1075 1080 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1085 1090 1095 Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1100 1105 1110 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1115 1120 1125 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser 1130 1135 1140 Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr 1145 1150 1155 Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1160 1165 1170 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 1175 1180 1185 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu 1190 1195 1200 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 1205 1210 1215 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1220 1225 1230 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1235 1240 1245 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 1250 1255 1260 Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 1265 1270 1275 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1280 1285 1290 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser 1295 1300 1305 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 1310 1315 1320 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1325 1330 1335 Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1340 1345 1350 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1355 1360 1365 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly 1370 1375 1380 Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr 1385 1390 1395 Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 1400 1405 1410 Glu Ser Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1415 1420 1425 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ala Ala Glu Pro 1430 1435 1440 Glu Ala 1445 <210> 34 <211> 1445 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 34 Ala Ser His His His His His His Ser Pro Ala Gly Ser Pro Thr Ser 1 5 10 15 Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 20 25 30 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 35 40 45 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 50 55 60 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 65 70 75 80 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 85 90 95 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 100 105 110 Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 115 120 125 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 130 135 140 Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 145 150 155 160 Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 165 170 175 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu 180 185 190 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 195 200 205 Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 210 215 220 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 225 230 235 240 Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 245 250 255 Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 260 265 270 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 275 280 285 Pro Ser Glu Gly Ser Ala Pro Gly Gly Ser Ala Pro Gly Val Arg Gly 290 295 300 Leu Thr Gly Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Asp Ile 305 310 315 320 Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly Asp Arg 325 330 335 Val Thr Ile Thr Cys Gln Ala Ser Gln Asp Ile Ser Asn Tyr Leu Asn 340 345 350 Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile Tyr Asp 355 360 365 Ala Ser Asn Leu Glu Thr Gly Val Pro Ser Arg Phe Ser Gly Ser Gly 370 375 380 Ser Gly Thr Asp Phe Thr Phe Thr Ile Ser Ser Leu Gln Pro Glu Asp 385 390 395 400 Ile Ala Thr Tyr Phe Cys Gln His Phe Asp His Leu Pro Leu Ala Phe 405 410 415 Gly Gly Gly Thr Lys Val Glu Ile Lys Gly Ala Thr Pro Pro Glu Thr 420 425 430 Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr Gly Gly Ser Ala Glu 435 440 445 Ser Glu Pro Pro Gly Glu Gly Gln Val Gln Leu Gln Glu Ser Gly Pro 450 455 460 Gly Leu Val Lys Pro Ser Glu Thr Leu Ser Leu Thr Cys Thr Val Ser 465 470 475 480 Gly Gly Ser Val Ser Ser Gly Asp Tyr Tyr Trp Thr Trp Ile Arg Gln 485 490 495 Ser Pro Gly Lys Gly Leu Glu Trp Ile Gly His Ile Tyr Tyr Ser Gly 500 505 510 Asn Thr Asn Tyr Asn Pro Ser Leu Lys Ser Arg Leu Thr Ile Ser Ile 515 520 525 Asp Thr Ser Lys Thr Gln Phe Ser Leu Lys Leu Ser Ser Val Thr Ala 530 535 540 Ala Asp Thr Ala Ile Tyr Tyr Cys Val Arg Asp Arg Val Thr Gly Ala 545 550 555 560 Phe Asp Ile Trp Gly Gln Gly Thr Met Val Thr Val Ser Ser Gly Gly 565 570 575 Gly Gly Ser Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser 580 585 590 Pro Gly Gly Thr Val Thr Leu Thr Cys Arg Ser Ser Thr Gly Ala Val 595 600 605 Thr Thr Ser Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala 610 615 620 Pro Arg Gly Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr Pro 625 630 635 640 Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu 645 650 655 Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Ala Leu Trp 660 665 670 Tyr Ser Asn Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 675 680 685 Gly Ala Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu 690 695 700 Thr Thr Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu Val 705 710 715 720 Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu 725 730 735 Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr Ala Met 740 745 750 Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg 755 760 765 Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Ser Val 770 775 780 Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr 785 790 795 800 Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys 805 810 815 Val Arg His Gly Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe Ala Tyr 820 825 830 Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Thr Ala Glu Ala 835 840 845 Ala Ser Ala Ser Gly Gly Val Arg Gly Leu Thr Gly Pro Pro Gly Ser 850 855 860 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala 865 870 875 880 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 885 890 895 Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr 900 905 910 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 915 920 925 Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 930 935 940 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser 945 950 955 960 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser 965 970 975 Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 980 985 990 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 995 1000 1005 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly 1010 1015 1020 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu 1025 1030 1035 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1040 1045 1050 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1055 1060 1065 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 1070 1075 1080 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1085 1090 1095 Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1100 1105 1110 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1115 1120 1125 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser 1130 1135 1140 Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr 1145 1150 1155 Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1160 1165 1170 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 1175 1180 1185 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu 1190 1195 1200 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 1205 1210 1215 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1220 1225 1230 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1235 1240 1245 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 1250 1255 1260 Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 1265 1270 1275 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1280 1285 1290 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser 1295 1300 1305 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 1310 1315 1320 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1325 1330 1335 Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1340 1345 1350 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1355 1360 1365 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly 1370 1375 1380 Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr 1385 1390 1395 Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 1400 1405 1410 Glu Ser Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1415 1420 1425 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ala Ala Glu Pro 1430 1435 1440 Glu Ala 1445 <210> 35 <211> 1445 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 35 Ala Ser His His His His His His Ser Pro Ala Gly Ser Pro Thr Ser 1 5 10 15 Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 20 25 30 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 35 40 45 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 50 55 60 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 65 70 75 80 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 85 90 95 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 100 105 110 Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 115 120 125 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 130 135 140 Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 145 150 155 160 Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 165 170 175 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu 180 185 190 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 195 200 205 Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 210 215 220 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 225 230 235 240 Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 245 250 255 Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 260 265 270 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 275 280 285 Pro Ser Glu Gly Ser Ala Pro Gly Gly Ser Ala Pro His Pro Val Glu 290 295 300 Leu Leu Ala Arg Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Asp Ile 305 310 315 320 Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly Asp Arg 325 330 335 Val Thr Ile Thr Cys Lys Ala Ser Gln Asp Val Ser Ile Gly Val Ala 340 345 350 Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile Tyr Ser 355 360 365 Ala Ser Tyr Arg Tyr Thr Gly Val Pro Ser Arg Phe Ser Gly Ser Gly 370 375 380 Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln Pro Glu Asp 385 390 395 400 Phe Ala Thr Tyr Tyr Cys Gln Gln Tyr Tyr Ile Tyr Pro Tyr Thr Phe 405 410 415 Gly Gln Gly Thr Lys Val Glu Ile Lys Gly Ala Thr Pro Pro Glu Thr 420 425 430 Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr Gly Gly Ser Ala Glu 435 440 445 Ser Glu Pro Pro Gly Glu Gly Glu Val Gln Leu Val Glu Ser Gly Gly 450 455 460 Gly Leu Val Gln Pro Gly Gly Ser Leu Arg Leu Ser Cys Ala Ala Ser 465 470 475 480 Gly Phe Thr Phe Thr Asp Tyr Thr Met Asp Trp Val Arg Gln Ala Pro 485 490 495 Gly Lys Gly Leu Glu Trp Val Ala Asp Val Asn Pro Asn Ser Gly Gly 500 505 510 Ser Ile Tyr Asn Gln Arg Phe Lys Gly Arg Phe Thr Leu Ser Val Asp 515 520 525 Arg Ser Lys Asn Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Ala Glu 530 535 540 Asp Thr Ala Val Tyr Cys Ala Arg Asn Leu Gly Pro Ser Phe Tyr 545 550 555 560 Phe Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Gly 565 570 575 Gly Gly Ser Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser 580 585 590 Pro Gly Gly Thr Val Thr Leu Thr Cys Arg Ser Ser Asn Gly Ala Val 595 600 605 Thr Ser Ser Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala 610 615 620 Pro Arg Gly Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr Pro 625 630 635 640 Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu 645 650 655 Ser Gly Val Gln Pro Glu Asp Glu Ala Val Tyr Tyr Cys Ala Leu Trp 660 665 670 Tyr Pro Asn Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 675 680 685 Gly Ala Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu 690 695 700 Thr Thr Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu Val 705 710 715 720 Gln Leu Leu Glu Ser Gly Gly Gly Ile Val Gln Pro Gly Gly Ser Leu 725 730 735 Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr Ala Met 740 745 750 Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg 755 760 765 Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Ser Val 770 775 780 Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Val Tyr 785 790 795 800 Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys 805 810 815 Val Arg His Glu Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe Ala His 820 825 830 Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Gly Thr Ala Glu Ala 835 840 845 Ala Ser Ala Ser Gly His Pro Val Glu Leu Leu Ala Arg Pro Gly Ser 850 855 860 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala 865 870 875 880 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 885 890 895 Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr 900 905 910 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 915 920 925 Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 930 935 940 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser 945 950 955 960 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser 965 970 975 Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 980 985 990 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 995 1000 1005 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly 1010 1015 1020 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu 1025 1030 1035 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1040 1045 1050 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1055 1060 1065 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 1070 1075 1080 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1085 1090 1095 Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1100 1105 1110 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1115 1120 1125 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser 1130 1135 1140 Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr 1145 1150 1155 Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1160 1165 1170 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 1175 1180 1185 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu 1190 1195 1200 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 1205 1210 1215 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1220 1225 1230 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1235 1240 1245 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 1250 1255 1260 Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 1265 1270 1275 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1280 1285 1290 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser 1295 1300 1305 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 1310 1315 1320 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1325 1330 1335 Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1340 1345 1350 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 1355 1360 1365 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly 1370 1375 1380 Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr 1385 1390 1395 Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 1400 1405 1410 Glu Ser Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 1415 1420 1425 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ala Ala Glu Pro 1430 1435 1440 Glu Ala 1445 <210> 36 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 36 Ile Gly Pro Gly Gly Val Ala Ala Ala Ala 1 5 10 <210> 37 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 37 Asp Pro Gln Gly Asp Ala Ala Gln 1 5 <210> 38 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 38 Asp Gly Val Arg Gly Leu Thr Gly Pro Ile 1 5 10 <210> 39 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 39 Arg Gly Pro Ser Gly His Met Gly Arg Glu 1 5 10 <210> 40 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 40 Ile Ser Pro Glu Ala Gln Ala Ala Ala Ala 1 5 10 <210> 41 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 41 Thr Pro Leu Gln Leu Phe Glu Gly 1 5 <210> 42 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 42 Gln Gly Pro Pro Gly Lys Asn Gly Glu Thr 1 5 10 <210> 43 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 43 Pro Pro Leu Gly Ala Pro Gly Leu 1 5 <210> 44 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 44 Lys Pro Leu Gly Asp Trp Ala Ala 1 5 <210> 45 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 45 Asp Gly Ala Ala Gly Val Lys Gly Asp Arg 1 5 10 <210> 46 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 46 Leu Leu Ser Ala Leu Val Glu Thr 1 5 <210> 47 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 47 Gln Pro Ala His Leu Thr Phe Pro 1 5 <210> 48 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 48 Asp His Pro Val Glu Leu Leu Ala Arg Asp 1 5 10 <210> 49 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 49 Gln Pro Ser Arg Leu Gln Asp Pro 1 5 <210> 50 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 50 Asp Gly Val Arg Gly Leu Thr Gly Pro Ile 1 5 10 <210> 51 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 51 Gln Pro Val Ser Leu Ala Asn Thr 1 5 <210> 52 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 52 Ile Gly Pro Gly Gly Val Ala Ala Ala Ala 1 5 10 <210> 53 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 53 Leu Thr Ser Asp Leu Gln Ala Gln 1 5 <210> 54 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 54 Ser Pro Leu Ser Leu Pro Val Thr 1 5 <210> 55 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 55 Gly Asp Pro Gly Glu Ile Leu Gly His Val 1 5 10 <210> 56 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 56 Ile Gly Pro Gly Gly Val Ala Ala Ala Ala 1 5 10 <210> 57 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 57 Thr Pro Leu Gln Leu Phe Glu Gly 1 5 <210> 58 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 58 Asp His Pro Val Glu Leu Leu Ala Arg Asp 1 5 10 <210> 59 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 59 Asp Gly Val Arg Gly Leu Thr Gly Pro Ile 1 5 10 <210> 60 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 60 Leu Pro Val Thr Leu Gly Gln Pro 1 5 <210> 61 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 61 Gln Pro Ala His Leu Thr Phe Pro 1 5 <210> 62 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 62 Ser Pro Val Thr Leu Gly Gln Pro 1 5 <210> 63 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 63 Gly Thr Leu Ser Leu Ser Pro Gly 1 5 <210> 64 <211> 9 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 64 Glu Glu Ala Pro Ser Leu Arg Pro Ala 1 5 <210> 65 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 65 Asp Gly Ala Ala Gly Val Lys Gly Asp Arg 1 5 10 <210> 66 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 66 Asp Gly Val Arg Gly Leu Thr Gly Pro Ile 1 5 10 <210> 67 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 67 Ile Gly Pro Gly Gly Val Ala Ala Ala Ala 1 5 10 <210> 68 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 68 Gln Gly Pro Pro Gly Lys Asn Gly Glu Thr 1 5 10 <210> 69 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 69 Arg Gly Pro Ser Gly His Met Gly Arg Glu 1 5 10 <210> 70 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 70 Asp Gly Ala Ala Gly Val Lys Gly Asp Arg 1 5 10 <210> 71 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 71 Lys Gly Ala Lys Gly Tyr Arg Gly Pro Glu 1 5 10 <210> 72 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 72 Pro Pro Leu Gly Ala Pro Gly Leu 1 5 <210> 73 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 73 Ile Gly Asn Arg Gly Pro Arg Gly Glu Thr 1 5 10 <210> 74 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 74 Gly Pro Gln Leu Arg Arg Gly Trp 1 5 <210> 75 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 75 Ser Pro Pro Gly Val Asp Ala Lys 1 5 <210> 76 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 76 Ala Ala Gly Ala Met Phe Leu Glu 1 5 <210> 77 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 77 Ala Ala Glu Ala Ile Ser Asp Ala 1 5 <210> 78 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 78 Glu Ala Ala Phe Phe Asp Thr Ala 1 5 <210> 79 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 79 Lys Ser His Ala Leu Gln Leu Asn 1 5 <210> 80 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 80 Ser Ala Arg Ala Ser Glu Ala Glu 1 5 <210> 81 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 81 Pro Ala Trp Ala Lys Glu Lys His 1 5 <210> 82 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 82 Ala Trp Ala Ala Glu Val Ile Ser 1 5 <210> 83 <211> 9 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 83 Glu Glu Ala Pro Ser Leu Arg Pro Ala 1 5 <210> 84 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 84 Ser Glu Ala Ser Tyr Glu Leu Thr 1 5 <210> 85 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 85 Pro Phe Thr Ala Ser Pro Ala Ser 1 5 <210> 86 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 86 Gln Pro Ser Arg Leu Gln Asp Pro 1 5 <210> 87 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 87 Leu Leu Ser Ala Leu Val Glu Thr 1 5 <210> 88 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 88 Gln Pro Ala His Leu Thr Phe Pro 1 5 <210> 89 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 89 Thr Pro Leu Gln Leu Phe Glu Gly 1 5 <210> 90 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 90 Gln Pro Val Ser Leu Ala Asn Thr 1 5 <210> 91 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 91 Asp Gly Val Arg Gly Leu Thr Gly Pro Ile 1 5 10 <210> 92 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 92 Asp His Pro Val Glu Leu Leu Ala Arg Asp 1 5 10 <210> 93 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 93 Ser Pro Leu Ser Leu Pro Val Thr 1 5 <210> 94 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 94 Leu Pro Val Thr Leu Gly Gln Pro 1 5 <210> 95 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 95 Ile Gly Pro Gly Gly Val Ala Ala Ala Ala 1 5 10 <210> 96 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 96 Arg Ser Gly Arg Asp Pro Asn His 1 5 <210> 97 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 97 Ala Ala Lys Arg Gly Pro Gly Gly 1 5 <210> 98 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 98 Arg Ser Lys Arg Asp Val Gly Ser 1 5 <210> 99 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 99 Val Ser Lys Arg Phe Pro Val Gly 1 5 <210> 100 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 100 Val Ser Ser Arg Ser Phe Phe Ser 1 5 <210> 101 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 101 Pro Val Gln Arg Ile Leu Gly Gly 1 5 <210> 102 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 102 Ser Ser Gly Pro Gly Ser Thr Gly 1 5 <210> 103 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 103 Phe Ser Ala Arg Gly His Arg Pro 1 5 <210> 104 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 104 Arg Gln Ile Arg Gly Leu Glu Glu 1 5 <210> 105 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 105 Arg Met Arg Arg Gly Ala Gly Gly 1 5 <210> 106 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 106 Arg Lys Lys Asn Ala Pro Pro Glu 1 5 <210> 107 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 107 Gly Asp Arg Asn Lys Pro Gly Val 1 5 <210> 108 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 108 Thr Gly Arg Asn Gly Phe Lys Ser 1 5 <210> 109 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 109 Gly Ser Trp Asn Ser Gly Ser Ser 1 5 <210> 110 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 110 Glu Pro Tyr Asn Ala Thr Leu Ser 1 5 <210> 111 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 111 Phe Thr Ala Asn Asp Ser Gly Pro 1 5 <210> 112 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 112 Gln Gly Val Asn Asp Asn Glu Glu 1 5 <210> 113 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 113 Ser Pro Arg Asn Pro Ser Ser Ala 1 5 <210> 114 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 114 Gln Gln Leu Asn Lys Pro Glu Val 1 5 <210> 115 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 115 Thr Ser Leu Asn Thr Val Gly Gly 1 5 <210> 116 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 116 Arg Met Arg Arg Gly Ala Gly Gly 1 5 <210> 117 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 117 Arg Ser Lys Arg Asp Val Gly Ser 1 5 <210> 118 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 118 Ala Ala Lys Arg Gly Pro Gly Gly 1 5 <210> 119 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 119 Arg Val Pro Arg Gln Val Arg Leu 1 5 <210> 120 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 120 Pro Val Gln Arg Ile Leu Gly Gly 1 5 <210> 121 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 121 Arg Lys Thr Arg Thr Val Val Gln 1 5 <210> 122 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 122 Pro Gly Leu Arg Ala Ala Pro Gly 1 5 <210> 123 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 123 Arg Gly Pro Arg Tyr Ala Glu Gly 1 5 <210> 124 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 124 Arg Gln Val Arg Thr Ile Val Glu 1 5 <210> 125 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 125 Arg Gln Ile Arg Gly Leu Glu Glu 1 5 <210> 126 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 126 Gly Glu Ser Pro Gly Gly Ser Ser Gly Ser Glu Ser 1 5 10 <210> 127 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 127 Gly Ser Glu Gly Ser Ser Gly Pro Gly Glu Ser Ser 1 5 10 <210> 128 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 128 Gly Ser Ser Glu Ser Gly Ser Ser Glu Gly Gly Pro 1 5 10 <210> 129 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 129 Gly Ser Gly Gly Glu Pro Ser Glu Ser Gly Ser Ser 1 5 10 <210> 130 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 130 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 1 5 10 <210> 131 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 131 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 1 5 10 <210> 132 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 132 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 1 5 10 <210> 133 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 133 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 1 5 10 <210> 134 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 134 Gly Ser Thr Ser Glu Ser Pro Ser Gly Thr Ala Pro 1 5 10 <210> 135 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 135 Gly Thr Ser Thr Pro Glu Ser Gly Ser Ala Ser Pro 1 5 10 <210> 136 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 136 Gly Thr Ser Pro Ser Gly Glu Ser Ser Thr Ala Pro 1 5 10 <210> 137 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 137 Gly Ser Thr Ser Ser Thr Ala Glu Ser Pro Gly Pro 1 5 10 <210> 138 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 138 Gly Thr Pro Gly Ser Gly Thr Ala Ser Ser Ser Pro 1 5 10 <210> 139 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 139 Gly Ser Ser Thr Pro Ser Gly Ala Thr Gly Ser Pro 1 5 10 <210> 140 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 140 Gly Ser Ser Pro Ser Ala Ser Thr Gly Thr Gly Pro 1 5 10 <210> 141 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 141 Gly Ala Ser Pro Gly Thr Ser Ser Thr Gly Ser Pro 1 5 10 <210> 142 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 142 Gly Glu Pro Ala Gly Ser Pro Thr Ser Thr Ser Glu 1 5 10 <210> 143 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 143 Gly Thr Gly Glu Pro Ser Ser Thr Pro Ala Ser Glu 1 5 10 <210> 144 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 144 Gly Ser Gly Pro Ser Thr Glu Ser Ala Pro Thr Glu 1 5 10 <210> 145 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 145 Gly Ser Glu Thr Pro Ser Gly Pro Ser Glu Thr Ala 1 5 10 <210> 146 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 146 Gly Pro Ser Glu Thr Ser Thr Ser Glu Pro Gly Ala 1 5 10 <210> 147 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 147 Gly Ser Pro Ser Glu Pro Thr Glu Gly Thr Ser Ala 1 5 10 <210> 148 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 148 Gly Ser Gly Ala Ser Glu Pro Thr Ser Thr Glu Pro 1 5 10 <210> 149 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 149 Gly Ser Glu Pro Ala Thr Ser Gly Thr Glu Pro Ser 1 5 10 <210> 150 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 150 Gly Thr Ser Glu Pro Ser Thr Ser Glu Pro Gly Ala 1 5 10 <210> 151 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 151 Gly Thr Ser Thr Glu Pro Ser Glu Pro Gly Ser Ala 1 5 10 <210> 152 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 152 Gly Ser Thr Ala Gly Ser Glu Thr Ser Thr Glu Ala 1 5 10 <210> 153 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 153 Gly Ser Glu Thr Ala Thr Ser Gly Ser Glu Thr Ala 1 5 10 <210> 154 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 154 Gly Thr Ser Glu Ser Ala Thr Ser Glu Ser Gly Ala 1 5 10 <210> 155 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 155 Gly Thr Ser Thr Glu Ala Ser Glu Gly Ser Ala Ser 1 5 10 <210> 156 <211> 144 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 156 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu 1 5 10 15 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 20 25 30 Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 35 40 45 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Glu Pro 50 55 60 Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly 65 70 75 80 Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 85 90 95 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu 100 105 110 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 115 120 125 Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 130 135 140 <210> 157 <211> 144 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 157 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser 1 5 10 15 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 20 25 30 Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 35 40 45 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 50 55 60 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 65 70 75 80 Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly 85 90 95 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly 100 105 110 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu 115 120 125 Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 130 135 140 <210> 158 <211> 144 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 158 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly 1 5 10 15 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly 20 25 30 Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 35 40 45 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu 50 55 60 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 65 70 75 80 Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly 85 90 95 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 100 105 110 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 115 120 125 Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 130 135 140 <210> 159 <211> 144 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 159 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly 1 5 10 15 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly 20 25 30 Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 35 40 45 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu 50 55 60 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 65 70 75 80 Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly 85 90 95 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 100 105 110 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 115 120 125 Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 130 135 140 <210> 160 <211> 144 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 160 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser 1 5 10 15 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 20 25 30 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 35 40 45 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 50 55 60 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 65 70 75 80 Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 85 90 95 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 100 105 110 Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser 115 120 125 Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 130 135 140 <210> 161 <211> 144 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 161 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser 1 5 10 15 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 20 25 30 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 35 40 45 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 50 55 60 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 65 70 75 80 Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 85 90 95 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 100 105 110 Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser 115 120 125 Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 130 135 140 <210> 162 <211> 144 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 162 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 1 5 10 15 Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 20 25 30 Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly 35 40 45 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu 50 55 60 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 65 70 75 80 Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 85 90 95 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly 100 105 110 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu 115 120 125 Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 130 135 140 <210> 163 <211> 144 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 163 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 1 5 10 15 Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 20 25 30 Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly 35 40 45 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu 50 55 60 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 65 70 75 80 Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 85 90 95 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly 100 105 110 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu 115 120 125 Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 130 135 140 <210> 164 <211> 144 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 164 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 1 5 10 15 Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 20 25 30 Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly 35 40 45 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu 50 55 60 Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser 65 70 75 80 Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 85 90 95 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 100 105 110 Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser 115 120 125 Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 130 135 140 <210> 165 <211> 144 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 165 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 1 5 10 15 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 20 25 30 Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 35 40 45 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala 50 55 60 Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser 65 70 75 80 Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 85 90 95 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Glu Pro Ala 100 105 110 Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 115 120 125 Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 130 135 140 <210> 166 <211> 288 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 166 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro 1 5 10 15 Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro 20 25 30 Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 35 40 45 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr 50 55 60 Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 65 70 75 80 Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 85 90 95 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu 100 105 110 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr 115 120 125 Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 130 135 140 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu 145 150 155 160 Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro 165 170 175 Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 180 185 190 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro 195 200 205 Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr 210 215 220 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 225 230 235 240 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Glu Pro 245 250 255 Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro 260 265 270 Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 275 280 285 <210> 167 <211> 288 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 167 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu 1 5 10 15 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 20 25 30 Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 35 40 45 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 50 55 60 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 65 70 75 80 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 85 90 95 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 100 105 110 Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 115 120 125 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 130 135 140 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro 145 150 155 160 Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro 165 170 175 Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 180 185 190 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr 195 200 205 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro 210 215 220 Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 225 230 235 240 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala 245 250 255 Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro 260 265 270 Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 275 280 285 <210> 168 <211> 576 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 168 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu 1 5 10 15 Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu 20 25 30 Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 35 40 45 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 50 55 60 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro 65 70 75 80 Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 85 90 95 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala 100 105 110 Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro 115 120 125 Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 130 135 140 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala 145 150 155 160 Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu 165 170 175 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 180 185 190 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr 195 200 205 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro 210 215 220 Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 225 230 235 240 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 245 250 255 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro 260 265 270 Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 275 280 285 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu 290 295 300 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 305 310 315 320 Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 325 330 335 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 340 345 350 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 355 360 365 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 370 375 380 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 385 390 395 400 Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 405 410 415 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 420 425 430 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro 435 440 445 Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro 450 455 460 Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 465 470 475 480 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr 485 490 495 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro 500 505 510 Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 515 520 525 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala 530 535 540 Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro 545 550 555 560 Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 565 570 575 <210> 169 <211> 625 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 169 Met Ala Glu Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Pro 1 5 10 15 Gly Ser Gly Thr Ala Ser Ser Ser Pro Gly Ser Ser Thr Pro Ser Gly 20 25 30 Ala Thr Gly Ser Pro Gly Ala Ser Pro Gly Thr Ser Ser Thr Gly Ser 35 40 45 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 50 55 60 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 65 70 75 80 Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 85 90 95 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 100 105 110 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 115 120 125 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 130 135 140 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro 145 150 155 160 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 165 170 175 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 180 185 190 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 195 200 205 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 210 215 220 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 225 230 235 240 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 245 250 255 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 260 265 270 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 275 280 285 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 290 295 300 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 305 310 315 320 Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 325 330 335 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 340 345 350 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 355 360 365 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 370 375 380 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 385 390 395 400 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 405 410 415 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 420 425 430 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 435 440 445 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 450 455 460 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 465 470 475 480 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 485 490 495 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 500 505 510 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 515 520 525 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 530 535 540 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 545 550 555 560 Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 565 570 575 Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro 580 585 590 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 595 600 605 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 610 615 620 Pro 625 <210> 170 <211> 864 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 170 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu 1 5 10 15 Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu 20 25 30 Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 35 40 45 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 50 55 60 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro 65 70 75 80 Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 85 90 95 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala 100 105 110 Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro 115 120 125 Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 130 135 140 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala 145 150 155 160 Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu 165 170 175 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 180 185 190 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr 195 200 205 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro 210 215 220 Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 225 230 235 240 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 245 250 255 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro 260 265 270 Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 275 280 285 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu 290 295 300 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 305 310 315 320 Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 325 330 335 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 340 345 350 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 355 360 365 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 370 375 380 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 385 390 395 400 Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 405 410 415 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 420 425 430 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro 435 440 445 Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro 450 455 460 Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 465 470 475 480 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr 485 490 495 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro 500 505 510 Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 515 520 525 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala 530 535 540 Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro 545 550 555 560 Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 565 570 575 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro 580 585 590 Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro 595 600 605 Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 610 615 620 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr 625 630 635 640 Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 645 650 655 Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 660 665 670 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu 675 680 685 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr 690 695 700 Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 705 710 715 720 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu 725 730 735 Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro 740 745 750 Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 755 760 765 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro 770 775 780 Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr 785 790 795 800 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 805 810 815 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Glu Pro 820 825 830 Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro 835 840 845 Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 850 855 860 <210> 171 <211> 865 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 171 Gly Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 1 5 10 15 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 20 25 30 Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 35 40 45 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 50 55 60 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 65 70 75 80 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 85 90 95 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro 100 105 110 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 115 120 125 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 130 135 140 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 145 150 155 160 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 165 170 175 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 180 185 190 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 195 200 205 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 210 215 220 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 225 230 235 240 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 245 250 255 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 260 265 270 Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 275 280 285 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 290 295 300 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 305 310 315 320 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 325 330 335 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 340 345 350 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 355 360 365 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 370 375 380 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 385 390 395 400 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 405 410 415 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 420 425 430 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 435 440 445 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 450 455 460 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 465 470 475 480 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 485 490 495 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 500 505 510 Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 515 520 525 Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro 530 535 540 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 545 550 555 560 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 565 570 575 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 580 585 590 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 595 600 605 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 610 615 620 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 625 630 635 640 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 645 650 655 Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 660 665 670 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 675 680 685 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro 690 695 700 Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 705 710 715 720 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 725 730 735 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 740 745 750 Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 755 760 765 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu 770 775 780 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro 785 790 795 800 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 805 810 815 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Glu 820 825 830 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 835 840 845 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 850 855 860 Pro 865 <210> 172 <211> 866 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 172 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 1 5 10 15 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 20 25 30 Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 35 40 45 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 50 55 60 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 65 70 75 80 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 85 90 95 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro 100 105 110 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 115 120 125 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 130 135 140 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 145 150 155 160 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 165 170 175 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 180 185 190 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 195 200 205 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 210 215 220 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 225 230 235 240 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 245 250 255 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 260 265 270 Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 275 280 285 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 290 295 300 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 305 310 315 320 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 325 330 335 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 340 345 350 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 355 360 365 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 370 375 380 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 385 390 395 400 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 405 410 415 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 420 425 430 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 435 440 445 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 450 455 460 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 465 470 475 480 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 485 490 495 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 500 505 510 Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 515 520 525 Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro 530 535 540 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 545 550 555 560 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 565 570 575 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 580 585 590 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 595 600 605 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 610 615 620 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 625 630 635 640 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 645 650 655 Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 660 665 670 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 675 680 685 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro 690 695 700 Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 705 710 715 720 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 725 730 735 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 740 745 750 Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 755 760 765 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu 770 775 780 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro 785 790 795 800 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 805 810 815 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Glu 820 825 830 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 835 840 845 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 850 855 860 Pro Gly 865 <210> 173 <211> 1152 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 173 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu 1 5 10 15 Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu 20 25 30 Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 35 40 45 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 50 55 60 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro 65 70 75 80 Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 85 90 95 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala 100 105 110 Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro 115 120 125 Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 130 135 140 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala 145 150 155 160 Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu 165 170 175 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 180 185 190 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr 195 200 205 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro 210 215 220 Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 225 230 235 240 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 245 250 255 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro 260 265 270 Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 275 280 285 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu 290 295 300 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 305 310 315 320 Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 325 330 335 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 340 345 350 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 355 360 365 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 370 375 380 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 385 390 395 400 Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 405 410 415 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 420 425 430 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro 435 440 445 Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro 450 455 460 Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 465 470 475 480 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr 485 490 495 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro 500 505 510 Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 515 520 525 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala 530 535 540 Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro 545 550 555 560 Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 565 570 575 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro 580 585 590 Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro 595 600 605 Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 610 615 620 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr 625 630 635 640 Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 645 650 655 Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 660 665 670 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu 675 680 685 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr 690 695 700 Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 705 710 715 720 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu 725 730 735 Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro 740 745 750 Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 755 760 765 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro 770 775 780 Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr 785 790 795 800 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 805 810 815 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Glu Pro 820 825 830 Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro 835 840 845 Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 850 855 860 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro 865 870 875 880 Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro 885 890 895 Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 900 905 910 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr 915 920 925 Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 930 935 940 Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 945 950 955 960 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu 965 970 975 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr 980 985 990 Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 995 1000 1005 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 1010 1015 1020 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala 1025 1030 1035 Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 1040 1045 1050 Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 1055 1060 1065 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro 1070 1075 1080 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro 1085 1090 1095 Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 1100 1105 1110 Ser Ala Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 1115 1120 1125 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 1130 1135 1140 Thr Glu Pro Ser Glu Gly Ser Ala Pro 1145 1150 <210> 174 <211> 144 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 174 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser 1 5 10 15 Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 20 25 30 Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser 35 40 45 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala 50 55 60 Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu 65 70 75 80 Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 85 90 95 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala 100 105 110 Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr 115 120 125 Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser 130 135 140 <210> 175 <211> 144 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 175 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 1 5 10 15 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 20 25 30 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 35 40 45 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly 50 55 60 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu 65 70 75 80 Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly 85 90 95 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly 100 105 110 Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser 115 120 125 Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 130 135 140 <210> 176 <211> 180 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 176 Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1 5 10 15 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 20 25 30 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro 35 40 45 Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 50 55 60 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 65 70 75 80 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 85 90 95 Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 100 105 110 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu 115 120 125 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro 130 135 140 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 145 150 155 160 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Glu 165 170 175 Pro Ala Thr Ser 180 <210> 177 <211> 216 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 177 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1 5 10 15 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 20 25 30 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 35 40 45 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 50 55 60 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro 65 70 75 80 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 85 90 95 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 100 105 110 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 115 120 125 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 130 135 140 Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 145 150 155 160 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 165 170 175 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 180 185 190 Glu Gly Ser Ala Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 195 200 205 Pro Gly Thr Ser Glu Ser Ala Thr 210 215 <210> 178 <211> 252 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 178 Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 1 5 10 15 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr 20 25 30 Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 35 40 45 Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 50 55 60 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu 65 70 75 80 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr 85 90 95 Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 100 105 110 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu 115 120 125 Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro 130 135 140 Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 145 150 155 160 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro 165 170 175 Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr 180 185 190 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 195 200 205 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Glu Pro 210 215 220 Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro 225 230 235 240 Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu 245 250 <210> 179 <211> 288 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 179 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 1 5 10 15 Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser 20 25 30 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala 35 40 45 Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu 50 55 60 Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 65 70 75 80 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser 85 90 95 Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 100 105 110 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 115 120 125 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser 130 135 140 Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr 145 150 155 160 Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 165 170 175 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala 180 185 190 Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 195 200 205 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser 210 215 220 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser 225 230 235 240 Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 245 250 255 Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser 260 265 270 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala 275 280 285 <210> 180 <211> 324 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 180 Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 1 5 10 15 Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro 20 25 30 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 35 40 45 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 50 55 60 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 65 70 75 80 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 85 90 95 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 100 105 110 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 115 120 125 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 130 135 140 Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 145 150 155 160 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 165 170 175 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro 180 185 190 Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 195 200 205 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 210 215 220 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 225 230 235 240 Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 245 250 255 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu 260 265 270 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro 275 280 285 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 290 295 300 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Glu 305 310 315 320 Pro Ala Thr Ser <210> 181 <211> 360 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 181 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1 5 10 15 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro 20 25 30 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro 35 40 45 Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 50 55 60 Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 65 70 75 80 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 85 90 95 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 100 105 110 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 115 120 125 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 130 135 140 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 145 150 155 160 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 165 170 175 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 180 185 190 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 195 200 205 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro 210 215 220 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 225 230 235 240 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 245 250 255 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 260 265 270 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 275 280 285 Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 290 295 300 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 305 310 315 320 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 325 330 335 Glu Gly Ser Ala Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 340 345 350 Pro Gly Thr Ser Glu Ser Ala Thr 355 360 <210> 182 <211> 360 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 182 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 1 5 10 15 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 20 25 30 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 35 40 45 Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 50 55 60 Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro 65 70 75 80 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 85 90 95 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 100 105 110 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 115 120 125 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 130 135 140 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 145 150 155 160 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 165 170 175 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 180 185 190 Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 195 200 205 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 210 215 220 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro 225 230 235 240 Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 245 250 255 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 260 265 270 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 275 280 285 Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 290 295 300 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu 305 310 315 320 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro 325 330 335 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 340 345 350 Pro Gly Thr Ser Thr Glu Pro Ser 355 360 <210> 183 <211> 432 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 183 Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 1 5 10 15 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 20 25 30 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 35 40 45 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 50 55 60 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 65 70 75 80 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 85 90 95 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 100 105 110 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro 115 120 125 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro 130 135 140 Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 145 150 155 160 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 165 170 175 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 180 185 190 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 195 200 205 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 210 215 220 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 225 230 235 240 Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 245 250 255 Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 260 265 270 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 275 280 285 Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 290 295 300 Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 305 310 315 320 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 325 330 335 Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 340 345 350 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 355 360 365 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser 370 375 380 Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 385 390 395 400 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 405 410 415 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Glu Pro Ala Thr Ser 420 425 430 <210> 184 <211> 468 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 184 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1 5 10 15 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 20 25 30 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 35 40 45 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 50 55 60 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 65 70 75 80 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 85 90 95 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 100 105 110 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 115 120 125 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro 130 135 140 Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 145 150 155 160 Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 165 170 175 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 180 185 190 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 195 200 205 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 210 215 220 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 225 230 235 240 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 245 250 255 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 260 265 270 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 275 280 285 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 290 295 300 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro 305 310 315 320 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro 325 330 335 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 340 345 350 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 355 360 365 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 370 375 380 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 385 390 395 400 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro 405 410 415 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 420 425 430 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 435 440 445 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 450 455 460 Glu Ser Ala Thr 465 <210> 185 <211> 504 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 185 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1 5 10 15 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 20 25 30 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 35 40 45 Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 50 55 60 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 65 70 75 80 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 85 90 95 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 100 105 110 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 115 120 125 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 130 135 140 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 145 150 155 160 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro 165 170 175 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro 180 185 190 Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 195 200 205 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 210 215 220 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 225 230 235 240 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 245 250 255 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 260 265 270 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 275 280 285 Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 290 295 300 Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 305 310 315 320 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 325 330 335 Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 340 345 350 Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 355 360 365 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 370 375 380 Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 385 390 395 400 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 405 410 415 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser 420 425 430 Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 435 440 445 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 450 455 460 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Glu Pro Ala Thr Ser 465 470 475 480 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 485 490 495 Pro Gly Thr Ser Thr Glu Pro Ser 500 <210> 186 <211> 540 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 186 Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr 1 5 10 15 Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser 20 25 30 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala 35 40 45 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 50 55 60 Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 65 70 75 80 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 85 90 95 Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 100 105 110 Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser 115 120 125 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro 130 135 140 Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 145 150 155 160 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 165 170 175 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr 180 185 190 Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 195 200 205 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 210 215 220 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser 225 230 235 240 Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr 245 250 255 Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr 260 265 270 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro 275 280 285 Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 290 295 300 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 305 310 315 320 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr 325 330 335 Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 340 345 350 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser 355 360 365 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala 370 375 380 Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu 385 390 395 400 Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser 405 410 415 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser 420 425 430 Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 435 440 445 Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 450 455 460 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala 465 470 475 480 Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu 485 490 495 Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser 500 505 510 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro 515 520 525 Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 530 535 540 <210> 187 <211> 576 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 187 Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 1 5 10 15 Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr 20 25 30 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr 35 40 45 Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 50 55 60 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 65 70 75 80 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 85 90 95 Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 100 105 110 Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 115 120 125 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser 130 135 140 Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 145 150 155 160 Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser 165 170 175 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala 180 185 190 Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu 195 200 205 Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 210 215 220 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala 225 230 235 240 Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr 245 250 255 Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser 260 265 270 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala 275 280 285 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 290 295 300 Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser 305 310 315 320 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala 325 330 335 Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu 340 345 350 Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 355 360 365 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser 370 375 380 Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 385 390 395 400 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 405 410 415 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser 420 425 430 Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr 435 440 445 Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 450 455 460 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala 465 470 475 480 Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 485 490 495 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser 500 505 510 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser 515 520 525 Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 530 535 540 Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser 545 550 555 560 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala 565 570 575 <210> 188 <211> 612 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 188 Gly Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1 5 10 15 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 20 25 30 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 35 40 45 Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 50 55 60 Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 65 70 75 80 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 85 90 95 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 100 105 110 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 115 120 125 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 130 135 140 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 145 150 155 160 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 165 170 175 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 180 185 190 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 195 200 205 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 210 215 220 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 225 230 235 240 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 245 250 255 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 260 265 270 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro 275 280 285 Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 290 295 300 Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 305 310 315 320 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 325 330 335 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 340 345 350 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 355 360 365 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 370 375 380 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 385 390 395 400 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 405 410 415 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 420 425 430 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 435 440 445 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro 450 455 460 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro 465 470 475 480 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 485 490 495 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 500 505 510 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 515 520 525 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 530 535 540 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro 545 550 555 560 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 565 570 575 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 580 585 590 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 595 600 605 Glu Ser Ala Thr 610 <210> 189 <211> 648 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 189 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1 5 10 15 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 20 25 30 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser 35 40 45 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 50 55 60 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 65 70 75 80 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro 85 90 95 Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 100 105 110 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 115 120 125 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 130 135 140 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 145 150 155 160 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 165 170 175 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 180 185 190 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 195 200 205 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 210 215 220 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 225 230 235 240 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 245 250 255 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 260 265 270 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 275 280 285 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 290 295 300 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro 305 310 315 320 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro 325 330 335 Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 340 345 350 Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 355 360 365 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 370 375 380 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 385 390 395 400 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 405 410 415 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 420 425 430 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 435 440 445 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 450 455 460 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 465 470 475 480 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 485 490 495 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro 500 505 510 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 515 520 525 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 530 535 540 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 545 550 555 560 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 565 570 575 Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 580 585 590 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 595 600 605 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 610 615 620 Glu Gly Ser Ala Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 625 630 635 640 Pro Gly Thr Ser Glu Ser Ala Thr 645 <210> 190 <211> 684 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 190 Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 1 5 10 15 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 20 25 30 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 35 40 45 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 50 55 60 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 65 70 75 80 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser 85 90 95 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 100 105 110 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 115 120 125 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro 130 135 140 Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 145 150 155 160 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 165 170 175 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 180 185 190 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 195 200 205 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 210 215 220 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 225 230 235 240 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 245 250 255 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 260 265 270 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 275 280 285 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 290 295 300 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 305 310 315 320 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 325 330 335 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 340 345 350 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro 355 360 365 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro 370 375 380 Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 385 390 395 400 Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 405 410 415 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 420 425 430 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 435 440 445 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 450 455 460 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 465 470 475 480 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 485 490 495 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 500 505 510 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 515 520 525 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 530 535 540 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro 545 550 555 560 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 565 570 575 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 580 585 590 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 595 600 605 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 610 615 620 Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 625 630 635 640 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 645 650 655 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 660 665 670 Glu Gly Ser Ala Pro Gly Ser Glu Pro Ala Thr Ser 675 680 <210> 191 <211> 720 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 191 Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 1 5 10 15 Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 20 25 30 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu 35 40 45 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 50 55 60 Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 65 70 75 80 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 85 90 95 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 100 105 110 Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 115 120 125 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 130 135 140 Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 145 150 155 160 Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 165 170 175 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser 180 185 190 Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser 195 200 205 Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 210 215 220 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 225 230 235 240 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 245 250 255 Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 260 265 270 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 275 280 285 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 290 295 300 Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 305 310 315 320 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu 325 330 335 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 340 345 350 Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly 355 360 365 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 370 375 380 Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 385 390 395 400 Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 405 410 415 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly 420 425 430 Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser 435 440 445 Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 450 455 460 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu 465 470 475 480 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 485 490 495 Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly 500 505 510 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 515 520 525 Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 530 535 540 Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 545 550 555 560 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser 565 570 575 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 580 585 590 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 595 600 605 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly 610 615 620 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly 625 630 635 640 Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 645 650 655 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser 660 665 670 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 675 680 685 Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly 690 695 700 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu 705 710 715 720 <210> 192 <211> 756 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 192 Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 1 5 10 15 Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 20 25 30 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu 35 40 45 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 50 55 60 Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 65 70 75 80 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 85 90 95 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 100 105 110 Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 115 120 125 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 130 135 140 Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 145 150 155 160 Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 165 170 175 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser 180 185 190 Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser 195 200 205 Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 210 215 220 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 225 230 235 240 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 245 250 255 Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 260 265 270 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 275 280 285 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 290 295 300 Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 305 310 315 320 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu 325 330 335 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 340 345 350 Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly 355 360 365 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 370 375 380 Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 385 390 395 400 Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 405 410 415 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly 420 425 430 Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser 435 440 445 Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 450 455 460 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu 465 470 475 480 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 485 490 495 Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly 500 505 510 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 515 520 525 Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 530 535 540 Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 545 550 555 560 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser 565 570 575 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 580 585 590 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 595 600 605 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly 610 615 620 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly 625 630 635 640 Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 645 650 655 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser 660 665 670 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 675 680 685 Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly 690 695 700 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu 705 710 715 720 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 725 730 735 Ser Ala Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly 740 745 750 Thr Ser Glu Ser 755 <210> 193 <211> 792 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 193 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 1 5 10 15 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu 20 25 30 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro 35 40 45 Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 50 55 60 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 65 70 75 80 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 85 90 95 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 100 105 110 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 115 120 125 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 130 135 140 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 145 150 155 160 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 165 170 175 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 180 185 190 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 195 200 205 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro 210 215 220 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 225 230 235 240 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 245 250 255 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 260 265 270 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 275 280 285 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 290 295 300 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 305 310 315 320 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 325 330 335 Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 340 345 350 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 355 360 365 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 370 375 380 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 385 390 395 400 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 405 410 415 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 420 425 430 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 435 440 445 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro 450 455 460 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro 465 470 475 480 Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 485 490 495 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 500 505 510 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 515 520 525 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 530 535 540 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 545 550 555 560 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 565 570 575 Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 580 585 590 Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 595 600 605 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 610 615 620 Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 625 630 635 640 Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 645 650 655 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 660 665 670 Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 675 680 685 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 690 695 700 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser 705 710 715 720 Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 725 730 735 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 740 745 750 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Glu Pro Ala Thr Ser 755 760 765 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 770 775 780 Pro Gly Thr Ser Thr Glu Pro Ser 785 790 <210> 194 <211> 828 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 194 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1 5 10 15 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 20 25 30 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 35 40 45 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 50 55 60 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu 65 70 75 80 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro 85 90 95 Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 100 105 110 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 115 120 125 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 130 135 140 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 145 150 155 160 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 165 170 175 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 180 185 190 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 195 200 205 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 210 215 220 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 225 230 235 240 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 245 250 255 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro 260 265 270 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 275 280 285 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 290 295 300 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 305 310 315 320 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 325 330 335 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 340 345 350 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 355 360 365 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 370 375 380 Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 385 390 395 400 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 405 410 415 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 420 425 430 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 435 440 445 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 450 455 460 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 465 470 475 480 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 485 490 495 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro 500 505 510 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro 515 520 525 Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 530 535 540 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 545 550 555 560 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 565 570 575 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 580 585 590 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 595 600 605 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 610 615 620 Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 625 630 635 640 Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 645 650 655 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 660 665 670 Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 675 680 685 Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 690 695 700 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 705 710 715 720 Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 725 730 735 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 740 745 750 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser 755 760 765 Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 770 775 780 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 785 790 795 800 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Glu Pro Ala Thr Ser 805 810 815 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 820 825 <210> 195 <211> 869 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 195 Gly Ser Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 1 5 10 15 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu 20 25 30 Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser 35 40 45 Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 50 55 60 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 65 70 75 80 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 85 90 95 Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly 100 105 110 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser 115 120 125 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 130 135 140 Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 145 150 155 160 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu 165 170 175 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 180 185 190 Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 195 200 205 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 210 215 220 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 225 230 235 240 Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 245 250 255 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 260 265 270 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 275 280 285 Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 290 295 300 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala 305 310 315 320 Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 325 330 335 Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 340 345 350 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 355 360 365 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 370 375 380 Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 385 390 395 400 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly 405 410 415 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly 420 425 430 Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 435 440 445 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 450 455 460 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 465 470 475 480 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 485 490 495 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser 500 505 510 Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser 515 520 525 Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Glu Gly 530 535 540 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser 545 550 555 560 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 565 570 575 Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 580 585 590 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 595 600 605 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 610 615 620 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 625 630 635 640 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly 645 650 655 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu 660 665 670 Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly 675 680 685 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly 690 695 700 Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser 705 710 715 720 Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 725 730 735 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser 740 745 750 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 755 760 765 Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly 770 775 780 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly 785 790 795 800 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly 805 810 815 Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 820 825 830 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 835 840 845 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 850 855 860 Ser Ala Pro Gly Arg 865 <210> 196 <211> 144 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 196 Ser Ala Gly Ser Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 1 5 10 15 Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 20 25 30 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 35 40 45 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 50 55 60 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 65 70 75 80 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 85 90 95 Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 100 105 110 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 115 120 125 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Glu Ser Ala Ser Arg 130 135 140 <210> 197 <211> 288 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 197 Ser Ala Gly Ser Pro Thr Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 1 5 10 15 Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 20 25 30 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu 35 40 45 Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu 50 55 60 Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 65 70 75 80 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro 85 90 95 Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro 100 105 110 Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 115 120 125 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr 130 135 140 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro 145 150 155 160 Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 165 170 175 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro 180 185 190 Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly 195 200 205 Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 210 215 220 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 225 230 235 240 Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Glu Pro Ala Thr Ser Gly 245 250 255 Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 260 265 270 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Ser Ala Ser Arg 275 280 285 <210> 198 <211> 432 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 198 Ser Ala Gly Ser Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 1 5 10 15 Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 20 25 30 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 35 40 45 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 50 55 60 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 65 70 75 80 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 85 90 95 Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 100 105 110 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 115 120 125 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 130 135 140 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 145 150 155 160 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 165 170 175 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 180 185 190 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 195 200 205 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 210 215 220 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 225 230 235 240 Gly Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 245 250 255 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 260 265 270 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 275 280 285 Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 290 295 300 Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 305 310 315 320 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 325 330 335 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 340 345 350 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 355 360 365 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 370 375 380 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 385 390 395 400 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 405 410 415 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Glu Ser Ala Ser Arg 420 425 430 <210> 199 <211> 576 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 199 Ser Ala Gly Ser Pro Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro 1 5 10 15 Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 20 25 30 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr 35 40 45 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 50 55 60 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 65 70 75 80 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 85 90 95 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 100 105 110 Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 115 120 125 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu 130 135 140 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 145 150 155 160 Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 165 170 175 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu 180 185 190 Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu 195 200 205 Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 210 215 220 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala 225 230 235 240 Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr 245 250 255 Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 260 265 270 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu 275 280 285 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 290 295 300 Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 305 310 315 320 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu 325 330 335 Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu 340 345 350 Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 355 360 365 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro 370 375 380 Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro 385 390 395 400 Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 405 410 415 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr 420 425 430 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro 435 440 445 Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 450 455 460 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro 465 470 475 480 Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly 485 490 495 Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 500 505 510 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 515 520 525 Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Glu Pro Ala Thr Ser Gly 530 535 540 Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 545 550 555 560 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Ser Ala Ser Arg 565 570 575 <210> 200 <211> 864 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 200 Ser Ala Gly Ser Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 1 5 10 15 Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 20 25 30 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 35 40 45 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 50 55 60 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 65 70 75 80 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 85 90 95 Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 100 105 110 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 115 120 125 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 130 135 140 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 145 150 155 160 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 165 170 175 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 180 185 190 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 195 200 205 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 210 215 220 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 225 230 235 240 Gly Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 245 250 255 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 260 265 270 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 275 280 285 Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 290 295 300 Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 305 310 315 320 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 325 330 335 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 340 345 350 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 355 360 365 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 370 375 380 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 385 390 395 400 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 405 410 415 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 420 425 430 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 435 440 445 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 450 455 460 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 465 470 475 480 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 485 490 495 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 500 505 510 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro 515 520 525 Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 530 535 540 Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 545 550 555 560 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 565 570 575 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 580 585 590 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 595 600 605 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 610 615 620 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 625 630 635 640 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 645 650 655 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 660 665 670 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 675 680 685 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro 690 695 700 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro 705 710 715 720 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 725 730 735 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 740 745 750 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 755 760 765 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 770 775 780 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro 785 790 795 800 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 805 810 815 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 820 825 830 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 835 840 845 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Glu Ser Ala Ser Arg 850 855 860 <210> 201 <211> 712 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 201 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 1 5 10 15 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 20 25 30 Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 35 40 45 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 50 55 60 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 65 70 75 80 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 85 90 95 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro 100 105 110 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 115 120 125 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 130 135 140 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 145 150 155 160 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 165 170 175 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 180 185 190 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 195 200 205 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 210 215 220 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 225 230 235 240 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 245 250 255 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 260 265 270 Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 275 280 285 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 290 295 300 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 305 310 315 320 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 325 330 335 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 340 345 350 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 355 360 365 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 370 375 380 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 385 390 395 400 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 405 410 415 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 420 425 430 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 435 440 445 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 450 455 460 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 465 470 475 480 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 485 490 495 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 500 505 510 Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 515 520 525 Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro 530 535 540 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 545 550 555 560 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 565 570 575 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 580 585 590 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 595 600 605 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 610 615 620 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 625 630 635 640 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 645 650 655 Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 660 665 670 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 675 680 685 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro 690 695 700 Thr Ser Thr Glu Ala His His His 705 710 <210> 202 <211> 864 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 202 Gly Ser Pro Gly Ala Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 1 5 10 15 Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 20 25 30 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 35 40 45 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 50 55 60 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 65 70 75 80 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 85 90 95 Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 100 105 110 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 115 120 125 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 130 135 140 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 145 150 155 160 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 165 170 175 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 180 185 190 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 195 200 205 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 210 215 220 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 225 230 235 240 Gly Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 245 250 255 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 260 265 270 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 275 280 285 Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 290 295 300 Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 305 310 315 320 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 325 330 335 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 340 345 350 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 355 360 365 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 370 375 380 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 385 390 395 400 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 405 410 415 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 420 425 430 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 435 440 445 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 450 455 460 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 465 470 475 480 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 485 490 495 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 500 505 510 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro 515 520 525 Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 530 535 540 Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 545 550 555 560 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 565 570 575 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 580 585 590 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 595 600 605 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 610 615 620 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 625 630 635 640 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 645 650 655 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 660 665 670 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 675 680 685 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro 690 695 700 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro 705 710 715 720 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 725 730 735 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 740 745 750 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 755 760 765 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 770 775 780 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro 785 790 795 800 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 805 810 815 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 820 825 830 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 835 840 845 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Glu Ser Ala Ser Arg 850 855 860 <210> 203 <211> 288 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 203 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser 1 5 10 15 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 20 25 30 Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 35 40 45 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 50 55 60 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 65 70 75 80 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 85 90 95 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly 100 105 110 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu 115 120 125 Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly 130 135 140 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly 145 150 155 160 Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser 165 170 175 Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 180 185 190 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser 195 200 205 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 210 215 220 Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly 225 230 235 240 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly 245 250 255 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly 260 265 270 Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 275 280 285 <210> 204 <211> 284 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 204 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro 1 5 10 15 Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro 20 25 30 Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 35 40 45 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr 50 55 60 Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 65 70 75 80 Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 85 90 95 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu 100 105 110 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr 115 120 125 Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 130 135 140 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu 145 150 155 160 Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro 165 170 175 Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 180 185 190 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro 195 200 205 Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr 210 215 220 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 225 230 235 240 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Glu Pro 245 250 255 Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro 260 265 270 Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu 275 280 <210> 205 <211> 292 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 205 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser 1 5 10 15 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 20 25 30 Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 35 40 45 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 50 55 60 Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser 65 70 75 80 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 85 90 95 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly 100 105 110 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu 115 120 125 Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly 130 135 140 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly 145 150 155 160 Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser 165 170 175 Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 180 185 190 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser 195 200 205 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 210 215 220 Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly 225 230 235 240 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly 245 250 255 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly 260 265 270 Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 275 280 285 Gly Ser Ala Pro 290 <210> 206 <211> 293 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 206 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 1 5 10 15 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 20 25 30 Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 35 40 45 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 50 55 60 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 65 70 75 80 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 85 90 95 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro 100 105 110 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 115 120 125 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 130 135 140 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 145 150 155 160 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 165 170 175 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 180 185 190 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 195 200 205 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 210 215 220 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 225 230 235 240 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 245 250 255 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 260 265 270 Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Gly Ala 275 280 285 Ala Glu Pro Glu Ala 290 <210> 207 <211> 300 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 207 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 1 5 10 15 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 20 25 30 Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 35 40 45 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 50 55 60 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 65 70 75 80 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 85 90 95 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro 100 105 110 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 115 120 125 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 130 135 140 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 145 150 155 160 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 165 170 175 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 180 185 190 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 195 200 205 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 210 215 220 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 225 230 235 240 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 245 250 255 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 260 265 270 Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 275 280 285 Pro Gly Ser Pro Ala Gly Ala Ala Glu Pro Glu Ala 290 295 300 <210> 208 <211> 864 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 208 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 1 5 10 15 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 20 25 30 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 35 40 45 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 50 55 60 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 65 70 75 80 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu 85 90 95 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro 100 105 110 Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 115 120 125 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 130 135 140 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 145 150 155 160 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 165 170 175 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 180 185 190 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 195 200 205 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 210 215 220 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 225 230 235 240 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 245 250 255 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 260 265 270 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro 275 280 285 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 290 295 300 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 305 310 315 320 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 325 330 335 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 340 345 350 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 355 360 365 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 370 375 380 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 385 390 395 400 Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 405 410 415 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 420 425 430 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 435 440 445 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 450 455 460 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 465 470 475 480 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 485 490 495 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 500 505 510 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro 515 520 525 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro 530 535 540 Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 545 550 555 560 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 565 570 575 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 580 585 590 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 595 600 605 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 610 615 620 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 625 630 635 640 Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 645 650 655 Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 660 665 670 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 675 680 685 Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 690 695 700 Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 705 710 715 720 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 725 730 735 Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 740 745 750 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 755 760 765 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser 770 775 780 Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 785 790 795 800 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 805 810 815 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Glu Pro Ala Thr Ser 820 825 830 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 835 840 845 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ala Ala Glu Pro Glu Ala 850 855 860 <210> 209 <211> 867 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 209 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu 1 5 10 15 Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu 20 25 30 Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 35 40 45 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 50 55 60 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro 65 70 75 80 Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 85 90 95 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala 100 105 110 Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro 115 120 125 Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 130 135 140 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala 145 150 155 160 Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu 165 170 175 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 180 185 190 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr 195 200 205 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro 210 215 220 Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 225 230 235 240 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 245 250 255 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro 260 265 270 Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 275 280 285 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu 290 295 300 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 305 310 315 320 Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 325 330 335 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 340 345 350 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 355 360 365 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 370 375 380 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 385 390 395 400 Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 405 410 415 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 420 425 430 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro 435 440 445 Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro 450 455 460 Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 465 470 475 480 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr 485 490 495 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro 500 505 510 Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 515 520 525 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala 530 535 540 Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro 545 550 555 560 Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 565 570 575 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro 580 585 590 Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro 595 600 605 Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 610 615 620 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr 625 630 635 640 Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 645 650 655 Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 660 665 670 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu 675 680 685 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr 690 695 700 Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 705 710 715 720 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu 725 730 735 Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro 740 745 750 Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 755 760 765 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro 770 775 780 Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr 785 790 795 800 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 805 810 815 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Glu Pro 820 825 830 Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro 835 840 845 Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ala Ala Glu 850 855 860 Pro Glu Ala 865 <210> 210 <211> 867 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 210 Ser Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr 1 5 10 15 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro 20 25 30 Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr 35 40 45 Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 50 55 60 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala 65 70 75 80 Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu 85 90 95 Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser 100 105 110 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala 115 120 125 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 130 135 140 Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser 145 150 155 160 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro 165 170 175 Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 180 185 190 Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 195 200 205 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala 210 215 220 Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu 225 230 235 240 Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 245 250 255 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala 260 265 270 Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 275 280 285 Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr 290 295 300 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr 305 310 315 320 Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 325 330 335 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 340 345 350 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 355 360 365 Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 370 375 380 Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 385 390 395 400 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser 405 410 415 Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 420 425 430 Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser 435 440 445 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala 450 455 460 Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu 465 470 475 480 Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 485 490 495 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala 500 505 510 Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr 515 520 525 Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser 530 535 540 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala 545 550 555 560 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 565 570 575 Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser 580 585 590 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala 595 600 605 Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu 610 615 620 Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 625 630 635 640 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser 645 650 655 Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 660 665 670 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 675 680 685 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser 690 695 700 Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr 705 710 715 720 Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 725 730 735 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala 740 745 750 Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 755 760 765 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser 770 775 780 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser 785 790 795 800 Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 805 810 815 Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser 820 825 830 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala 835 840 845 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 850 855 860 Ala Pro Gly 865 <210> 211 <211> 868 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 211 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 1 5 10 15 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 20 25 30 Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 35 40 45 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 50 55 60 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 65 70 75 80 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 85 90 95 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro 100 105 110 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 115 120 125 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 130 135 140 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 145 150 155 160 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 165 170 175 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 180 185 190 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 195 200 205 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 210 215 220 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 225 230 235 240 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 245 250 255 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 260 265 270 Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 275 280 285 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 290 295 300 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 305 310 315 320 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 325 330 335 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 340 345 350 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 355 360 365 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 370 375 380 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 385 390 395 400 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 405 410 415 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 420 425 430 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 435 440 445 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 450 455 460 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 465 470 475 480 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 485 490 495 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 500 505 510 Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 515 520 525 Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro 530 535 540 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 545 550 555 560 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 565 570 575 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 580 585 590 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 595 600 605 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 610 615 620 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 625 630 635 640 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 645 650 655 Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 660 665 670 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 675 680 685 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro 690 695 700 Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 705 710 715 720 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 725 730 735 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 740 745 750 Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 755 760 765 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu 770 775 780 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro 785 790 795 800 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 805 810 815 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Glu 820 825 830 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 835 840 845 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ala Ala 850 855 860 Glu Pro Glu Ala 865 <210> 212 <211> 584 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 212 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 1 5 10 15 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 20 25 30 Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 35 40 45 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 50 55 60 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 65 70 75 80 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 85 90 95 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro 100 105 110 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 115 120 125 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 130 135 140 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 145 150 155 160 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 165 170 175 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 180 185 190 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 195 200 205 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 210 215 220 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 225 230 235 240 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 245 250 255 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 260 265 270 Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 275 280 285 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 290 295 300 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 305 310 315 320 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 325 330 335 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 340 345 350 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 355 360 365 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 370 375 380 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 385 390 395 400 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 405 410 415 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 420 425 430 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 435 440 445 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 450 455 460 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 465 470 475 480 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 485 490 495 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 500 505 510 Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 515 520 525 Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro 530 535 540 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 545 550 555 560 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 565 570 575 Pro Gly Ala Ala Glu Pro Glu Ala 580 <210> 213 <211> 874 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 213 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 1 5 10 15 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 20 25 30 Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 35 40 45 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 50 55 60 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 65 70 75 80 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 85 90 95 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro 100 105 110 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 115 120 125 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 130 135 140 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 145 150 155 160 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 165 170 175 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 180 185 190 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 195 200 205 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 210 215 220 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 225 230 235 240 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 245 250 255 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 260 265 270 Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 275 280 285 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 290 295 300 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 305 310 315 320 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 325 330 335 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 340 345 350 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 355 360 365 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 370 375 380 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 385 390 395 400 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 405 410 415 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 420 425 430 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 435 440 445 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 450 455 460 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 465 470 475 480 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 485 490 495 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 500 505 510 Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 515 520 525 Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro 530 535 540 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 545 550 555 560 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 565 570 575 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 580 585 590 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 595 600 605 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 610 615 620 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 625 630 635 640 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 645 650 655 Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 660 665 670 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 675 680 685 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro 690 695 700 Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 705 710 715 720 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 725 730 735 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 740 745 750 Pro Glu Ser Gly Pro Gly Phe Thr Ala Asx Thr Ser Glu Ser Ala Thr 755 760 765 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Pro Thr Glu 770 775 780 Ser Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro 785 790 795 800 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 805 810 815 Glu Gly Ser Ala Pro Gly Thr Glu Ser Thr Pro Ser Glu Gly Ser Ala 820 825 830 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 835 840 845 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 850 855 860 Glu Gly Ser Ala Pro Gly Glu Pro Glu Ala 865 870 <210> 214 <211> 870 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 214 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 1 5 10 15 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 20 25 30 Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 35 40 45 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 50 55 60 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 65 70 75 80 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 85 90 95 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro 100 105 110 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 115 120 125 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 130 135 140 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 145 150 155 160 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 165 170 175 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 180 185 190 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 195 200 205 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 210 215 220 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 225 230 235 240 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 245 250 255 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 260 265 270 Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 275 280 285 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 290 295 300 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 305 310 315 320 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 325 330 335 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 340 345 350 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 355 360 365 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 370 375 380 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 385 390 395 400 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 405 410 415 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 420 425 430 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 435 440 445 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 450 455 460 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 465 470 475 480 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 485 490 495 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 500 505 510 Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 515 520 525 Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro 530 535 540 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 545 550 555 560 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 565 570 575 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 580 585 590 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 595 600 605 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 610 615 620 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 625 630 635 640 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 645 650 655 Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 660 665 670 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 675 680 685 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro 690 695 700 Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 705 710 715 720 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 725 730 735 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 740 745 750 Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 755 760 765 Pro Gly Ser Glu Pro Ala Thr Ser Gly Pro Thr Glu Ser Gly Ser Glu 770 775 780 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro 785 790 795 800 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 805 810 815 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Glu 820 825 830 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 835 840 845 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 850 855 860 Pro Gly Glu Pro Glu Ala 865 870 <210> 215 <211> 870 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 215 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 1 5 10 15 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 20 25 30 Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 35 40 45 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 50 55 60 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 65 70 75 80 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 85 90 95 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro 100 105 110 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 115 120 125 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 130 135 140 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 145 150 155 160 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 165 170 175 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 180 185 190 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 195 200 205 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 210 215 220 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 225 230 235 240 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 245 250 255 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 260 265 270 Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 275 280 285 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 290 295 300 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 305 310 315 320 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 325 330 335 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 340 345 350 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 355 360 365 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 370 375 380 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 385 390 395 400 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 405 410 415 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 420 425 430 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 435 440 445 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 450 455 460 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 465 470 475 480 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 485 490 495 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 500 505 510 Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 515 520 525 Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro 530 535 540 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 545 550 555 560 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 565 570 575 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 580 585 590 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 595 600 605 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 610 615 620 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 625 630 635 640 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 645 650 655 Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 660 665 670 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 675 680 685 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro 690 695 700 Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 705 710 715 720 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 725 730 735 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 740 745 750 Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 755 760 765 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu 770 775 780 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro 785 790 795 800 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 805 810 815 Pro Gly Thr Glu Ser Thr Pro Ser Glu Gly Ser Ala Pro Gly Ser Glu 820 825 830 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 835 840 845 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 850 855 860 Pro Gly Glu Pro Glu Ala 865 870 <210> 216 <211> 294 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 216 Ala Ser Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Ser Gly Thr Ser 1 5 10 15 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Glu Thr Glu Pro Ser 20 25 30 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 35 40 45 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 50 55 60 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Thr Pro Ala Glu Ser 65 70 75 80 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 85 90 95 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 100 105 110 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 115 120 125 Pro Glu Ser Gly Pro Gly Glu Ser Pro Ala Thr Ser Gly Ser Thr Pro 130 135 140 Glu Ser Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro 145 150 155 160 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro 165 170 175 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 180 185 190 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 195 200 205 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 210 215 220 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 225 230 235 240 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro 245 250 255 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 260 265 270 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 275 280 285 Pro Gly Gly Ser Ala Pro 290 <210> 217 <211> 294 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 217 Ala Ser Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Ser Gly Thr Ser 1 5 10 15 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 20 25 30 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 35 40 45 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 50 55 60 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 65 70 75 80 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 85 90 95 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 100 105 110 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 115 120 125 Pro Glu Ser Gly Pro Gly Glu Ser Pro Ala Thr Ser Gly Ser Thr Pro 130 135 140 Glu Ser Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro 145 150 155 160 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro 165 170 175 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 180 185 190 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 195 200 205 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 210 215 220 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 225 230 235 240 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro 245 250 255 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 260 265 270 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 275 280 285 Pro Gly Gly Ser Ala Pro 290 <210> 218 <211> 294 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 218 Ala Ser Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Ser Gly Thr Ser 1 5 10 15 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 20 25 30 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 35 40 45 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 50 55 60 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Thr Pro Ala Glu Ser 65 70 75 80 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 85 90 95 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 100 105 110 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 115 120 125 Pro Glu Ser Gly Pro Gly Glu Glu Pro Ala Thr Ser Gly Ser Thr Pro 130 135 140 Glu Ser Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro 145 150 155 160 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro 165 170 175 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 180 185 190 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 195 200 205 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 210 215 220 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 225 230 235 240 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro 245 250 255 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 260 265 270 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 275 280 285 Pro Gly Gly Ser Ala Pro 290 <210> 219 <211> 294 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 219 Ala Ser Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Ser Gly Thr Ser 1 5 10 15 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 20 25 30 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 35 40 45 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 50 55 60 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Thr Pro Ala Glu Ser 65 70 75 80 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 85 90 95 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 100 105 110 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 115 120 125 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 130 135 140 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro 145 150 155 160 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro 165 170 175 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 180 185 190 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 195 200 205 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 210 215 220 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 225 230 235 240 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro 245 250 255 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 260 265 270 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 275 280 285 Pro Gly Gly Ser Ala Pro 290 <210> 220 <211> 866 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 220 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 1 5 10 15 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 20 25 30 Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 35 40 45 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 50 55 60 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 65 70 75 80 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 85 90 95 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro 100 105 110 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 115 120 125 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 130 135 140 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 145 150 155 160 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 165 170 175 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 180 185 190 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 195 200 205 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 210 215 220 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 225 230 235 240 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 245 250 255 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 260 265 270 Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 275 280 285 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 290 295 300 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 305 310 315 320 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 325 330 335 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 340 345 350 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 355 360 365 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 370 375 380 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 385 390 395 400 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 405 410 415 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 420 425 430 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 435 440 445 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 450 455 460 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 465 470 475 480 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 485 490 495 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 500 505 510 Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 515 520 525 Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro 530 535 540 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 545 550 555 560 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 565 570 575 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 580 585 590 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 595 600 605 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 610 615 620 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 625 630 635 640 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 645 650 655 Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 660 665 670 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 675 680 685 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro 690 695 700 Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 705 710 715 720 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 725 730 735 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 740 745 750 Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 755 760 765 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu 770 775 780 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro 785 790 795 800 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 805 810 815 Pro Gly Thr Glu Ser Thr Pro Ser Glu Gly Ser Ala Pro Gly Ser Glu 820 825 830 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 835 840 845 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 850 855 860 Pro Gly 865 <210> 221 <211> 578 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 221 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 1 5 10 15 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 20 25 30 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 35 40 45 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 50 55 60 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 65 70 75 80 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 85 90 95 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 100 105 110 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 115 120 125 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 130 135 140 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 145 150 155 160 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 165 170 175 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 180 185 190 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 195 200 205 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 210 215 220 Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 225 230 235 240 Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro 245 250 255 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 260 265 270 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 275 280 285 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 290 295 300 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 305 310 315 320 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 325 330 335 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 340 345 350 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 355 360 365 Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 370 375 380 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 385 390 395 400 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro 405 410 415 Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 420 425 430 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 435 440 445 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 450 455 460 Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 465 470 475 480 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu 485 490 495 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro 500 505 510 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 515 520 525 Pro Gly Thr Glu Ser Thr Pro Ser Glu Gly Ser Ala Pro Gly Ser Glu 530 535 540 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 545 550 555 560 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 565 570 575 Pro Gly <210> 222 <211> 1152 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 222 Ser Ala Gly Ser Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 1 5 10 15 Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 20 25 30 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 35 40 45 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 50 55 60 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 65 70 75 80 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Thr Pro Ala Glu Ser 85 90 95 Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 100 105 110 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 115 120 125 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 130 135 140 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 145 150 155 160 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 165 170 175 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 180 185 190 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 195 200 205 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 210 215 220 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 225 230 235 240 Gly Ser Thr Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 245 250 255 Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 260 265 270 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala 275 280 285 Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr 290 295 300 Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser 305 310 315 320 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala 325 330 335 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 340 345 350 Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 355 360 365 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 370 375 380 Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 385 390 395 400 Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser 405 410 415 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro 420 425 430 Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 435 440 445 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 450 455 460 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr 465 470 475 480 Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 485 490 495 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 500 505 510 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser 515 520 525 Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr 530 535 540 Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr 545 550 555 560 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro 565 570 575 Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 580 585 590 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 595 600 605 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr 610 615 620 Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 625 630 635 640 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser 645 650 655 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala 660 665 670 Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu 675 680 685 Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser 690 695 700 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser 705 710 715 720 Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 725 730 735 Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 740 745 750 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala 755 760 765 Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu 770 775 780 Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser 785 790 795 800 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro 805 810 815 Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 820 825 830 Ala Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 835 840 845 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro 850 855 860 Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr 865 870 875 880 Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 885 890 895 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser 900 905 910 Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 915 920 925 Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 930 935 940 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr 945 950 955 960 Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu 965 970 975 Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr 980 985 990 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro 995 1000 1005 Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 1010 1015 1020 Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 1025 1030 1035 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 1040 1045 1050 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala 1055 1060 1065 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 1070 1075 1080 Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 1085 1090 1095 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 1100 1105 1110 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 1115 1120 1125 Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 1130 1135 1140 Ser Gly Pro Gly Thr Glu Ser Ala Ser 1145 1150 <210> 223 <211> 1153 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 223 Ser Ala Gly Ser Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 1 5 10 15 Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 20 25 30 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 35 40 45 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 50 55 60 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 65 70 75 80 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 85 90 95 Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 100 105 110 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 115 120 125 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 130 135 140 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 145 150 155 160 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 165 170 175 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 180 185 190 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 195 200 205 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 210 215 220 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 225 230 235 240 Gly Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 245 250 255 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 260 265 270 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 275 280 285 Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 290 295 300 Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 305 310 315 320 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 325 330 335 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 340 345 350 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 355 360 365 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 370 375 380 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 385 390 395 400 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 405 410 415 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 420 425 430 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 435 440 445 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 450 455 460 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 465 470 475 480 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 485 490 495 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 500 505 510 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro 515 520 525 Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 530 535 540 Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 545 550 555 560 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 565 570 575 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 580 585 590 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 595 600 605 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 610 615 620 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 625 630 635 640 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 645 650 655 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 660 665 670 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 675 680 685 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro 690 695 700 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro 705 710 715 720 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 725 730 735 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 740 745 750 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 755 760 765 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 770 775 780 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro 785 790 795 800 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 805 810 815 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 820 825 830 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 835 840 845 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 850 855 860 Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 865 870 875 880 Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 885 890 895 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 900 905 910 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 915 920 925 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 930 935 940 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 945 950 955 960 Gly Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Thr Glu 965 970 975 Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr 980 985 990 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro 995 1000 1005 Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 1010 1015 1020 Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 1025 1030 1035 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ala 1040 1045 1050 Thr Glu Ser Pro Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala 1055 1060 1065 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 1070 1075 1080 Ser Ala Pro Gly Thr Ser Ala Glu Ser Ala Thr Pro Glu Ser Gly 1085 1090 1095 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 1100 1105 1110 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu 1115 1120 1125 Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro 1130 1135 1140 Glu Ser Gly Pro Gly Thr Glu Ser Ala Ser 1145 1150 <210> 224 <211> 864 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 224 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu 1 5 10 15 Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu 20 25 30 Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 35 40 45 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 50 55 60 Glu Pro Ser Glu Gly Ser Ala Pro Ala Thr Ser Glu Ser Ala Thr Pro 65 70 75 80 Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 85 90 95 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala 100 105 110 Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Ser Pro 115 120 125 Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 130 135 140 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala 145 150 155 160 Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu 165 170 175 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 180 185 190 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr 195 200 205 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro 210 215 220 Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 225 230 235 240 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 245 250 255 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro 260 265 270 Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 275 280 285 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu 290 295 300 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 305 310 315 320 Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 325 330 335 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 340 345 350 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 355 360 365 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 370 375 380 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 385 390 395 400 Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 405 410 415 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 420 425 430 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro 435 440 445 Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro 450 455 460 Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 465 470 475 480 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr 485 490 495 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro 500 505 510 Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 515 520 525 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala 530 535 540 Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro 545 550 555 560 Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 565 570 575 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro 580 585 590 Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro 595 600 605 Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 610 615 620 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr 625 630 635 640 Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 645 650 655 Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 660 665 670 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu 675 680 685 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr 690 695 700 Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 705 710 715 720 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu 725 730 735 Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro 740 745 750 Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 755 760 765 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro 770 775 780 Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr 785 790 795 800 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 805 810 815 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Glu Pro 820 825 830 Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro 835 840 845 Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 850 855 860 <210> 225 <211> 864 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 225 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu 1 5 10 15 Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu 20 25 30 Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 35 40 45 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 50 55 60 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro 65 70 75 80 Glu Ser Gly Pro Gly Ser Glu Ser Ala Thr Ser Gly Ser Glu Thr Pro 85 90 95 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala 100 105 110 Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro 115 120 125 Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 130 135 140 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala 145 150 155 160 Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu 165 170 175 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 180 185 190 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr 195 200 205 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro 210 215 220 Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 225 230 235 240 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 245 250 255 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro 260 265 270 Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 275 280 285 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu 290 295 300 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 305 310 315 320 Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 325 330 335 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 340 345 350 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 355 360 365 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 370 375 380 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 385 390 395 400 Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 405 410 415 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 420 425 430 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro 435 440 445 Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro 450 455 460 Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 465 470 475 480 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr 485 490 495 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro 500 505 510 Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 515 520 525 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala 530 535 540 Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro 545 550 555 560 Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 565 570 575 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro 580 585 590 Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro 595 600 605 Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 610 615 620 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr 625 630 635 640 Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr 645 650 655 Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 660 665 670 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu 675 680 685 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr 690 695 700 Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 705 710 715 720 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu 725 730 735 Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro 740 745 750 Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 755 760 765 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu Pro 770 775 780 Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr 785 790 795 800 Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 805 810 815 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Glu Pro 820 825 830 Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro 835 840 845 Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 850 855 860 <210> 226 <211> 292 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 226 Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Ser Gly Thr Ser Glu Ser 1 5 10 15 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly 20 25 30 Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 35 40 45 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser 50 55 60 Ala Thr Pro Glu Ser Gly Pro Gly Ser Thr Pro Ala Glu Ser Gly Ser 65 70 75 80 Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly 85 90 95 Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly 100 105 110 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu 115 120 125 Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly 130 135 140 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly 145 150 155 160 Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser 165 170 175 Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 180 185 190 Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser 195 200 205 Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu 210 215 220 Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly 225 230 235 240 Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly 245 250 255 Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly 260 265 270 Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly 275 280 285 Gly Ser Ala Pro 290 <210> 227 <211> 582 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 227 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 1 5 10 15 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 20 25 30 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 35 40 45 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 50 55 60 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 65 70 75 80 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 85 90 95 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 100 105 110 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 115 120 125 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 130 135 140 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 145 150 155 160 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 165 170 175 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 180 185 190 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 195 200 205 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 210 215 220 Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 225 230 235 240 Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro 245 250 255 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 260 265 270 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 275 280 285 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 290 295 300 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 305 310 315 320 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 325 330 335 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 340 345 350 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 355 360 365 Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 370 375 380 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 385 390 395 400 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro 405 410 415 Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 420 425 430 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 435 440 445 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 450 455 460 Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 465 470 475 480 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Glu 485 490 495 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro 500 505 510 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 515 520 525 Pro Gly Thr Glu Ser Thr Pro Ser Glu Gly Ser Ala Pro Gly Ser Glu 530 535 540 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 545 550 555 560 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 565 570 575 Pro Gly Glu Pro Glu Ala 580 <210> 228 <211> 576 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 228 Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 1 5 10 15 Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr 20 25 30 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr 35 40 45 Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 50 55 60 Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 65 70 75 80 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro 85 90 95 Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 100 105 110 Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 115 120 125 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser 130 135 140 Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 145 150 155 160 Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser 165 170 175 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala 180 185 190 Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu 195 200 205 Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 210 215 220 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala 225 230 235 240 Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr 245 250 255 Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser 260 265 270 Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala 275 280 285 Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 290 295 300 Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser 305 310 315 320 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala 325 330 335 Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu 340 345 350 Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr 355 360 365 Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser 370 375 380 Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 385 390 395 400 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr 405 410 415 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser 420 425 430 Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr 435 440 445 Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr 450 455 460 Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala 465 470 475 480 Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser 485 490 495 Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser 500 505 510 Glu Ser Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser 515 520 525 Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser 530 535 540 Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser 545 550 555 560 Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala 565 570 575 <210> 229 <211> 576 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 229 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu 1 5 10 15 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 20 25 30 Ser Glu Thr Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro 35 40 45 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu 50 55 60 Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu 65 70 75 80 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 85 90 95 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr 100 105 110 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 115 120 125 Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 130 135 140 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu 145 150 155 160 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 165 170 175 Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 180 185 190 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu 195 200 205 Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro 210 215 220 Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 225 230 235 240 Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro 245 250 255 Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro 260 265 270 Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 275 280 285 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr 290 295 300 Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu 305 310 315 320 Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro 325 330 335 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala 340 345 350 Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu 355 360 365 Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 370 375 380 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu 385 390 395 400 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 405 410 415 Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 420 425 430 Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu 435 440 445 Ser Ala Ser Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr 450 455 460 Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu 465 470 475 480 Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu 485 490 495 Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu 500 505 510 Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 515 520 525 Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu 530 535 540 Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly 545 550 555 560 Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro 565 570 575 <210> 230 <211> 576 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 230 Gly Ser Glu Thr Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 1 5 10 15 Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 20 25 30 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 35 40 45 Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 50 55 60 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 65 70 75 80 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 85 90 95 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 100 105 110 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 115 120 125 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Thr Glu Pro Ser 130 135 140 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 145 150 155 160 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 165 170 175 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro 180 185 190 Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 195 200 205 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 210 215 220 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 225 230 235 240 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 245 250 255 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 260 265 270 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 275 280 285 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 290 295 300 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 305 310 315 320 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 325 330 335 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 340 345 350 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 355 360 365 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 370 375 380 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 385 390 395 400 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro 405 410 415 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro 420 425 430 Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 435 440 445 Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 450 455 460 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 465 470 475 480 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Thr Glu 485 490 495 Thr Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 500 505 510 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 515 520 525 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 530 535 540 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 545 550 555 560 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 565 570 575 <210> 231 <211> 576 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 231 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 1 5 10 15 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 20 25 30 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 35 40 45 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 50 55 60 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 65 70 75 80 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 85 90 95 Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 100 105 110 Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser 115 120 125 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser 130 135 140 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 145 150 155 160 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 165 170 175 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser 180 185 190 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 195 200 205 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 210 215 220 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 225 230 235 240 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 245 250 255 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 260 265 270 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 275 280 285 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 290 295 300 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 305 310 315 320 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr 325 330 335 Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 340 345 350 Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro 355 360 365 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 370 375 380 Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 385 390 395 400 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Glu 405 410 415 Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr 420 425 430 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 435 440 445 Pro Gly Thr Ser Glu Ser Ala Ser Pro Glu Ser Gly Pro Gly Thr Ser 450 455 460 Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro Ala Gly Ser Pro 465 470 475 480 Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 485 490 495 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 500 505 510 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro Ala Gly Ser Pro 515 520 525 Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu 530 535 540 Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Thr Ser 545 550 555 560 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 565 570 575 <210> 232 <211> 294 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 232 Ala Ser Ser Pro Ala Gly Ser Pro Thr Ser Thr Glu Ser Gly Thr Ser 1 5 10 15 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Thr Glu Pro Ser 20 25 30 Glu Gly Ser Ala Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 35 40 45 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Thr Ser 50 55 60 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Thr Pro Ala Glu Ser 65 70 75 80 Gly Ser Glu Thr Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly 85 90 95 Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala Pro Gly Ser Pro 100 105 110 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Glu Ser Ala Thr 115 120 125 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 130 135 140 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Ser Pro 145 150 155 160 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Ser Pro Ala Gly Ser Pro 165 170 175 Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 180 185 190 Pro Gly Thr Ser Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser 195 200 205 Glu Ser Ala Thr Pro Glu Ser Gly Pro Gly Thr Ser Glu Ser Ala Thr 210 215 220 Pro Glu Ser Gly Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr 225 230 235 240 Pro Gly Ser Glu Pro Ala Thr Ser Gly Ser Glu Thr Pro Gly Ser Pro 245 250 255 Ala Gly Ser Pro Thr Ser Thr Glu Glu Gly Thr Ser Thr Glu Pro Ser 260 265 270 Glu Gly Ser Ala Pro Gly Thr Ser Thr Glu Pro Ser Glu Gly Ser Ala 275 280 285 Pro Gly Gly Ser Ala Pro 290 <210> 233 <211> 52 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 233 Tyr Arg Gln Ser Met Asn Asn Phe Gln Gly Leu Arg Ser Phe Gly Cys 1 5 10 15 Arg Phe Gly Thr Cys Thr Val Gln Lys Leu Ala His Gln Ile Tyr Gln 20 25 30 Phe Thr Asp Lys Asp Lys Asp Asn Val Ala Pro Arg Ser Lys Ile Ser 35 40 45 Pro Gln Gly Tyr 50 <210> 234 <211> 37 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 234 Lys Cys Asn Thr Ala Thr Cys Ala Thr Gln Arg Leu Ala Asn Phe Leu 1 5 10 15 Val Arg Ser Ser Asn Asn Leu Gly Pro Val Leu Pro Pro Thr Asn Val 20 25 30 Gly Ser Asn Thr Tyr 35 <210> 235 <211> 37 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 235 Lys Cys Asn Thr Ala Thr Cys Ala Thr Gln Arg Leu Ala Asn Phe Leu 1 5 10 15 Val His Ser Ser Asn Asn Phe Gly Ala Ile Leu Ser Ser Thr Asn Val 20 25 30 Gly Ser Asn Thr Tyr 35 <210> 236 <211> 32 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 236 Cys Gly Asn Leu Ser Thr Cys Met Leu Gly Thr Tyr Thr Gln Asp Phe 1 5 10 15 Asn Lys Phe His Thr Phe Pro Gln Thr Ala Ile Gly Val Gly Ala Pro 20 25 30 <210> 237 <211> 32 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 237 Cys Ser Asn Leu Ser Thr Cys Val Leu Gly Lys Leu Ser Gln Glu Leu 1 5 10 15 His Lys Leu Gln Thr Tyr Pro Arg Thr Asn Thr Gly Ser Gly Thr Pro 20 25 30 <210> 238 <211> 36 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 238 Ala Cys Asp Thr Ala Thr Cys Val Thr His Arg Leu Ala Gly Leu Leu 1 5 10 15 Ser Arg Ser Gly Gly Val Val Lys Asn Met Val Pro Thr Asn Val Gly 20 25 30 Ser Lys Ala Phe 35 <210> 239 <211> 37 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 239 Ala Cys Asn Thr Ala Thr Cys Val Thr His Arg Leu Ala Gly Leu Leu 1 5 10 15 Ser Arg Ser Gly Gly Met Val Lys Ser Asn Phe Val Pro Thr Asn Val 20 25 30 Gly Ser Lys Ala Phe 35 <210> 240 <211> 115 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 240 Met Asn Ser Gly Val Cys Leu Cys Val Leu Met Ala Val Leu Ala Ala 1 5 10 15 Gly Ala Leu Thr Gln Pro Val Pro Pro Ala Asp Pro Ala Gly Ser Gly 20 25 30 Leu Gln Arg Ala Glu Glu Ala Pro Arg Arg Gln Leu Arg Val Ser Gln 35 40 45 Arg Thr Asp Gly Glu Ser Arg Ala His Leu Gly Ala Leu Leu Ala Arg 50 55 60 Tyr Ile Gln Gln Ala Arg Lys Ala Pro Ser Gly Arg Met Ser Ile Val 65 70 75 80 Lys Asn Leu Gln Asn Leu Asp Pro Ser His Arg Ile Ser Asp Arg Asp 85 90 95 Tyr Met Gly Trp Met Asp Phe Gly Arg Arg Ser Ala Glu Glu Tyr Glu 100 105 110 Tyr Pro Ser 115 <210> 241 <211> 33 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 241 Lys Ala Pro Ser Gly Arg Met Ser Ile Val Lys Asn Leu Gln Asn Leu 1 5 10 15 Asp Pro Ser His Arg Ile Ser Asp Arg Asp Tyr Met Gly Trp Met Asp 20 25 30 Phe <210> 242 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 242 Asp Tyr Met Gly Trp Met Asp Phe 1 5 <210> 243 <211> 39 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 243 His Ser Asp Gly Thr Phe Thr Ser Asp Leu Ser Lys Gln Met Glu Glu 1 5 10 15 Glu Ala Val Arg Leu Phe Ile Glu Trp Leu Lys Asn Gly Gly Pro Ser 20 25 30 Ser Gly Ala Pro Pro Pro Ser 35 <210> 244 <211> 39 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 244 His Gly Glu Gly Thr Phe Thr Ser Asp Leu Ser Lys Gln Met Glu Glu 1 5 10 15 Glu Ala Val Arg Leu Phe Ile Glu Trp Leu Lys Asn Gly Gly Pro Ser 20 25 30 Ser Gly Ala Pro Pro Pro Ser 35 <210> 245 <211> 216 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 245 Met Arg Ser Gly Cys Val Val Val His Val Trp Ile Leu Ala Gly Leu 1 5 10 15 Trp Leu Ala Val Ala Gly Arg Pro Leu Ala Phe Ser Asp Ala Gly Pro 20 25 30 His Val His Tyr Gly Trp Gly Asp Pro Ile Arg Leu Arg His Leu Tyr 35 40 45 Thr Ser Gly Pro His Gly Leu Ser Ser Cys Phe Leu Arg Ile Arg Ala 50 55 60 Asp Gly Val Val Asp Cys Ala Arg Gly Gln Ser Ala His Ser Leu Leu 65 70 75 80 Glu Ile Lys Ala Val Ala Leu Arg Thr Val Ala Ile Lys Gly Val His 85 90 95 Ser Val Arg Tyr Leu Cys Met Gly Ala Asp Gly Lys Met Gln Gly Leu 100 105 110 Leu Gln Tyr Ser Glu Glu Asp Cys Ala Phe Glu Glu Glu Ile Arg Pro 115 120 125 Asp Gly Tyr Asn Val Tyr Arg Ser Glu Lys His Arg Leu Pro Val Ser 130 135 140 Leu Ser Ser Ala Lys Gln Arg Gln Leu Tyr Lys Asn Arg Gly Phe Leu 145 150 155 160 Pro Leu Ser His Phe Leu Pro Met Leu Pro Met Val Pro Glu Glu Pro 165 170 175 Glu Asp Leu Arg Gly His Leu Glu Ser Asp Met Phe Ser Ser Pro Leu 180 185 190 Glu Thr Asp Ser Met Asp Pro Phe Gly Leu Val Thr Gly Leu Glu Ala 195 200 205 Val Arg Ser Pro Ser Phe Glu Lys 210 215 <210> 246 <211> 209 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 246 Met Asp Ser Asp Glu Thr Gly Phe Glu His Ser Gly Leu Trp Val Ser 1 5 10 15 Val Leu Ala Gly Leu Leu Leu Gly Ala Cys Gln Ala His Pro Ile Pro 20 25 30 Asp Ser Ser Pro Leu Leu Gln Phe Gly Gly Gln Val Arg Gln Arg Tyr 35 40 45 Leu Tyr Thr Asp Asp Ala Gln Gln Thr Glu Ala His Leu Glu Ile Arg 50 55 60 Glu Asp Gly Thr Val Gly Gly Ala Ala Asp Gln Ser Pro Glu Ser Leu 65 70 75 80 Leu Gln Leu Lys Ala Leu Lys Pro Gly Val Ile Gln Ile Leu Gly Val 85 90 95 Lys Thr Ser Arg Phe Leu Cys Gln Arg Pro Asp Gly Ala Leu Tyr Gly 100 105 110 Ser Leu His Phe Asp Pro Glu Ala Cys Ser Phe Arg Glu Leu Leu Leu 115 120 125 Glu Asp Gly Tyr Asn Val Tyr Gln Ser Glu Ala His Gly Leu Pro Leu 130 135 140 His Leu Pro Gly Asn Lys Ser Pro His Arg Asp Pro Ala Pro Arg Gly 145 150 155 160 Pro Ala Arg Phe Leu Pro Leu Pro Gly Leu Pro Pro Ala Leu Pro Glu 165 170 175 Pro Pro Gly Ile Leu Ala Pro Gln Pro Pro Asp Val Gly Ser Ser Asp 180 185 190 Pro Leu Ser Met Val Gly Pro Ser Gln Gly Arg Ser Pro Ser Tyr Ala 195 200 205 Ser <210> 247 <211> 34 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 247 Gln Leu Gly Pro Gln Gly Pro Pro His Leu Val Ala Asp Pro Ser Lys 1 5 10 15 Lys Gln Gly Pro Trp Leu Glu Glu Glu Glu Glu Ala Tyr Gly Trp Met 20 25 30 Asp Phe <210> 248 <211> 22 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 248 Asp Pro Ser Lys Lys Gln Gly Pro Trp Leu Glu Glu Glu Glu Glu Ala 1 5 10 15 Tyr Gly Trp Met Asp Phe 20 <210> 249 <211> 42 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 249 Tyr Ala Glu Gly Thr Phe Ile Ser Asp Tyr Ser Ile Ala Met Asp Lys 1 5 10 15 Ile His Gln Gln Asp Phe Val Asn Trp Leu Leu Ala Gln Lys Gly Lys 20 25 30 Lys Asn Asp Trp Lys His Asn Ile Thr Gln 35 40 <210> 250 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 250 Gly Ser Ser Phe Leu Ser Pro Glu His Gln Arg Val Gln Gln Arg Lys 1 5 10 15 Glu Ser Lys Lys Pro Pro Ala Lys Leu Gln Pro Arg 20 25 <210> 251 <211> 29 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 251 His Ser Gln Gly Thr Phe Thr Ser Asp Tyr Ser Lys Tyr Leu Asp Ser 1 5 10 15 Arg Arg Ala Gln Asp Phe Val Gln Trp Leu Met Asn Thr 20 25 <210> 252 <211> 37 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 252 His Asp Glu Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val 1 5 10 15 Ser Ser Thr Leu Glu Gly Gln Ala Ala Leu Glu Phe Ile Ala Trp Leu 20 25 30 Val Lys Gly Arg Gly 35 <210> 253 <211> 30 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 253 His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Leu Glu Phe Ile Ala Trp Leu Val Lys Gly Arg 20 25 30 <210> 254 <211> 31 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 254 His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Thr Leu Glu Gly 1 5 10 15 Gln Ala Ala Leu Glu Phe Ile Ala Trp Leu Val Lys Gly Arg Gly 20 25 30 <210> 255 <211> 37 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 255 His Ala Glu Gly Thr Tyr Thr Asn Asp Val Thr Glu Tyr Leu Glu Glu 1 5 10 15 Lys Ala Ala Lys Glu Phe Ile Glu Trp Leu Ile Lys Gly Lys Pro Lys 20 25 30 Lys Ile Arg Tyr Ser 35 <210> 256 <211> 33 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 256 His Ala Asp Gly Ser Phe Ser Asp Glu Met Asn Thr Ile Leu Asp Asn 1 5 10 15 Leu Ala Ala Arg Asp Phe Ile Asn Trp Leu Ile Glu Thr Lys Ile Thr 20 25 30 Asp <210> 257 <211> 31 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 257 His Ala Glu Gly Thr Phe Thr Asn Asp Met Thr Asn Tyr Leu Glu Glu 1 5 10 15 Lys Ala Ala Lys Glu Phe Val Gly Trp Leu Ile Lys Gly Arg Pro 20 25 30 <210> 258 <211> 70 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 258 Gly Pro Glu Thr Leu Cys Gly Ala Glu Leu Val Asp Ala Leu Gln Phe 1 5 10 15 Val Cys Gly Asp Arg Gly Phe Tyr Phe Asn Lys Pro Thr Gly Tyr Gly 20 25 30 Ser Ser Ser Arg Arg Ala Pro Gln Thr Gly Ile Val Asp Glu Cys Cys 35 40 45 Phe Arg Ser Cys Asp Leu Arg Arg Leu Glu Met Tyr Cys Ala Pro Leu 50 55 60 Lys Pro Ala Lys Ser Ala 65 70 <210> 259 <211> 67 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 259 Ala Tyr Arg Pro Ser Glu Thr Leu Cys Gly Gly Glu Leu Val Asp Thr 1 5 10 15 Leu Gln Phe Val Cys Gly Asp Arg Gly Phe Tyr Phe Ser Arg Pro Ala 20 25 30 Ser Arg Val Ser Arg Arg Ser Arg Gly Ile Val Glu Glu Cys Cys Phe 35 40 45 Arg Ser Cys Asp Leu Ala Leu Leu Glu Thr Tyr Cys Ala Thr Pro Ala 50 55 60 Lys Ser Glu 65 <210> 260 <211> 149 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 260 Glu Glu Ser Gln Lys Lys Leu Pro Ser Ser Arg Ile Thr Cys Pro Gln 1 5 10 15 Gly Ser Val Ala Tyr Gly Ser Tyr Cys Tyr Ser Leu Ile Leu Ile Pro 20 25 30 Gln Thr Trp Ser Asn Ala Glu Leu Ser Cys Gln Met His Phe Ser Gly 35 40 45 His Leu Ala Phe Leu Leu Ser Thr Gly Glu Ile Thr Phe Val Ser Ser 50 55 60 Leu Val Lys Asn Ser Leu Thr Ala Tyr Gln Tyr Ile Trp Ile Gly Leu 65 70 75 80 His Asp Pro Ser His Gly Thr Leu Pro Asn Gly Ser Gly Trp Lys Trp 85 90 95 Ser Ser Ser Asn Val Leu Thr Phe Tyr Asn Trp Glu Arg Asn Pro Ser 100 105 110 Ile Ala Ala Asp Arg Gly Tyr Cys Ala Val Leu Ser Gln Lys Ser Gly 115 120 125 Phe Gln Lys Trp Arg Asp Phe Asn Cys Glu Asn Glu Leu Pro Tyr Ile 130 135 140 Cys Lys Phe Lys Val 145 <210> 261 <211> 47 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 261 Thr Gln Ala Gln Leu Leu Arg Val Gly Cys Val Leu Gly Thr Cys Gln 1 5 10 15 Val Gln Asn Leu Ser His Arg Leu Trp Gln Leu Met Gly Pro Ala Gly 20 25 30 Arg Gln Asp Ser Ala Pro Val Asp Pro Ser Ser Pro His Ser Tyr 35 40 45 <210> 262 <211> 146 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 262 Val Pro Ile Gln Lys Val Gln Asp Asp Thr Lys Thr Leu Ile Lys Thr 1 5 10 15 Ile Val Thr Arg Ile Asn Asp Ile Ser His Thr Gln Ser Val Ser Ser 20 25 30 Lys Gln Lys Val Thr Gly Leu Asp Phe Ile Pro Gly Leu His Pro Ile 35 40 45 Leu Thr Leu Ser Lys Met Asp Gln Thr Leu Ala Val Tyr Gln Gln Ile 50 55 60 Leu Thr Ser Met Pro Ser Arg Asn Val Ile Gln Ile Ser Asn Asp Leu 65 70 75 80 Glu Asn Leu Arg Asp Leu Leu His Val Leu Ala Phe Ser Lys Ser Cys 85 90 95 His Leu Pro Trp Ala Ser Gly Leu Glu Thr Leu Asp Ser Leu Gly Gly 100 105 110 Val Leu Glu Ala Ser Gly Tyr Ser Thr Glu Val Val Ala Leu Ser Arg 115 120 125 Leu Gln Gly Ser Leu Gln Asp Met Leu Trp Gln Leu Asp Leu Ser Pro 130 135 140 Gly Cys 145 <210> 263 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 263 Tyr Phe Leu Phe Arg Pro Arg Asn 1 5 <210> 264 <211> 9 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 264 Gly Tyr Phe Leu Phe Arg Pro Arg Asn 1 5 <210> 265 <211> 25 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 265 Phe Arg Val Asp Glu Glu Phe Gln Ser Pro Phe Ala Ser Gln Ser Arg 1 5 10 15 Gly Tyr Phe Leu Phe Arg Pro Arg Asn 20 25 <210> 266 <211> 25 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 266 Phe Lys Val Asp Glu Glu Phe Gln Gly Pro Ile Val Ser Gln Asn Arg 1 5 10 15 Arg Tyr Phe Leu Phe Arg Pro Arg Asn 20 25 <210> 267 <211> 33 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 267 Ile Leu Gln Arg Gly Ser Gly Thr Ala Ala Val Asp Phe Thr Lys Lys 1 5 10 15 Asp His Thr Ala Thr Trp Gly Arg Pro Phe Phe Leu Phe Arg Pro Arg 20 25 30 Asn <210> 268 <211> 23 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 268 Tyr Lys Val Asn Glu Tyr Gln Gly Pro Val Ala Pro Ser Gly Gly Phe 1 5 10 15 Phe Leu Phe Arg Pro Arg Asn 20 <210> 269 <211> 37 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 269 His Ser Gln Gly Thr Phe Thr Ser Asp Tyr Ser Lys Tyr Leu Asp Ser 1 5 10 15 Arg Arg Ala Gln Asp Phe Val Gln Trp Leu Met Asn Thr Lys Arg Asn 20 25 30 Arg Asn Asn Ile Ala 35 <210> 270 <211> 36 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 270 Tyr Pro Ile Lys Pro Glu Ala Pro Gly Glu Asp Ala Ser Pro Glu Glu 1 5 10 15 Leu Asn Arg Tyr Tyr Ala Ser Leu Arg His Tyr Leu Asn Leu Val Thr 20 25 30 Arg Gln Arg Tyr 35 <210> 271 <211> 37 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 271 Lys Cys Asn Thr Ala Thr Cys Ala Thr Asn Arg Leu Ala Asn Phe Leu 1 5 10 15 Val His Ser Ser Asn Asn Phe Gly Pro Ile Leu Pro Pro Thr Asn Val 20 25 30 Gly Ser Asn Thr Tyr 35 <210> 272 <211> 40 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 272 Asp Asn Pro Ser Leu Ser Ile Asp Leu Thr Phe His Leu Leu Arg Thr 1 5 10 15 Leu Leu Glu Leu Ala Arg Thr Gln Ser Gln Arg Glu Arg Ala Glu Gln 20 25 30 Asn Arg Ile Ile Phe Asp Ser Val 35 40 <210> 273 <211> 41 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 273 Ile Val Leu Ser Leu Asp Val Pro Ile Gly Leu Leu Gln Ile Leu Leu 1 5 10 15 Glu Gln Ala Arg Ala Arg Ala Ala Arg Glu Gln Ala Thr Thr Asn Ala 20 25 30 Arg Ile Leu Ala Arg Val Gly His Cys 35 40 <210> 274 <211> 38 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 274 Phe Thr Leu Ser Leu Asp Val Pro Thr Asn Ile Met Asn Leu Leu Phe 1 5 10 15 Asn Ile Ala Lys Ala Lys Asn Leu Arg Ala Gln Ala Ala Ala Asn Ala 20 25 30 His Leu Met Ala Gln Ile 35 <210> 275 <211> 37 <212> PRT <213> artificial sequence <220> <223> synthetic <220> <221> MISC_FEATURE <222> (10)..(10) <223> X is N or Q <220> <221> MISC_FEATURE <222> (25)..(25) <223> X is S, P, or G <220> <221> MISC_FEATURE <222> (28)..(28) <223> X is S, P, or G <220> <221> MISC_FEATURE <222> (29)..(29) <223> X is S, P, or G <400> 275 Lys Cys Asn Thr Ala Thr Cys Ala Thr Xaa Arg Leu Ala Asn Phe Leu 1 5 10 15 Val His Ser Ser Asn Asn Phe Gly Xaa Ile Leu Xaa Xaa Thr Asn Val 20 25 30 Gly Ser Asn Thr Tyr 35 <210> 276 <211> 37 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 276 Lys Cys Asn Thr Ala Thr Cys Ala Thr Asn Arg Leu Ala Asn Phe Leu 1 5 10 15 Val His Ser Ser Asn Asn Phe Gly Gly Ile Leu Gly Gly Thr Asn Val 20 25 30 Gly Ser Asn Thr Tyr 35 <210> 277 <211> 37 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 277 His Ala Glu Gly Thr Tyr Thr Asn Asp Val Thr Glu Tyr Leu Glu Glu 1 5 10 15 Lys Ala Ala Lys Glu Phe Ile Glu Trp Leu Ile Lys Gly Lys Pro Lys 20 25 30 Lys Ile Arg Tyr Ser 35 <210> 278 <211> 37 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 278 His Ala Glu Gly Thr Phe Thr Ser Asp Val Thr Gln Gln Leu Asp Glu 1 5 10 15 Lys Ala Ala Lys Glu Phe Ile Asp Trp Leu Ile Asn Gly Gly Pro Ser 20 25 30 Lys Glu Ile Ile Ser 35 <210> 279 <211> 33 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 279 His Ala Glu Gly Thr Tyr Thr Asn Asp Val Thr Glu Tyr Leu Glu Glu 1 5 10 15 Lys Ala Ala Lys Glu Phe Ile Ile Glu Trp Leu Ile Lys Gly Lys Pro 20 25 30 Lys <210> 280 <211> 32 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 280 His Ala Glu Gly Thr Phe Thr Asn Asp Met Thr Asn Tyr Leu Glu Glu 1 5 10 15 Lys Ala Ala Lys Glu Phe Val Gly Trp Leu Ile Lys Gly Arg Pro Lys 20 25 30 <210> 281 <211> 27 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 281 His Ala Glu Gly Thr Phe Ile Ser Asp Tyr Ser Ile Ala Met Asp Lys 1 5 10 15 Ile Arg Gln Gln Asp Phe Val Asn Trp Leu Leu 20 25 <210> 282 <211> 27 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 282 His Ala Glu Gly Thr Phe Ile Ser Asp Tyr Ser Ile Ala Met Asp Lys 1 5 10 15 Ile Arg Gln Gln Asp Phe Val Asn Trp Leu Leu 20 25 <210> 283 <211> 32 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 283 His Ala Asp Gly Thr Phe Thr Asn Asp Met Thr Ser Tyr Leu Asp Ala 1 5 10 15 Lys Ala Ala Arg Asp Phe Val Ser Trp Leu Ala Arg Ser Asp Lys Ser 20 25 30 <210> 284 <211> 30 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 284 His Ala Glu Gly Thr Tyr Thr Ser Asp Val Ser Ser Tyr Leu Gln Asp 1 5 10 15 Gln Ala Ala Lys Glu Phe Val Ser Trp Leu Lys Thr Gly Arg 20 25 30 <210> 285 <211> 30 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 285 His Ala Glu Gly Thr Tyr Thr Ser Asp Val Ser Ser Tyr Leu Gln Asp 1 5 10 15 Gln Ala Ala Lys Glu Phe Val Ser Trp Leu Lys Thr Gly Arg 20 25 30 <210> 286 <211> 38 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 286 His Ala Asp Gly Ile Tyr Thr Ser Asp Val Ala Ser Leu Thr Asp Tyr 1 5 10 15 Leu Lys Ser Lys Arg Phe Val Glu Ser Leu Ser Asn Tyr Asn Lys Arg 20 25 30 Gln Asn Asp Arg Arg Met 35 <210> 287 <211> 31 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 287 Tyr Ala Asp Ala Pro Tyr Ile Ser Asp Val Tyr Ser Tyr Leu Gln Asp 1 5 10 15 Gln Val Ala Lys Lys Trp Leu Lys Ser Gly Gln Asp Arg Arg Glu 20 25 30 <210> 288 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 288 His Ala Asp Gly Thr Tyr Thr Ser Asp Val Ser Ser Tyr Leu Gln Glu 1 5 10 15 Gln Ala Ala Lys Asp Phe Ile Thr Trp Leu Lys Ser 20 25 <210> 289 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 289 His Ala Glu Gly Thr Tyr Thr Ser Asp Val Ser Ser Tyr Leu Gln Asp 1 5 10 15 Gln Ala Ala Lys Glu Phe Val Ser Trp Leu Lys Thr 20 25 <210> 290 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 290 His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Lys Glu Phe Ile Ala Trp Leu Val Lys 20 25 <210> 291 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 291 His Ala Asp Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Lys Asp 1 5 10 15 Gln Ala Ile Lys Asp Phe Val Asp Arg Leu Lys Ala 20 25 <210> 292 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 292 His Ala Asp Gly Ile Tyr Thr Ser Asp Val Ala Ser Leu Thr Asp Tyr 1 5 10 15 Leu Lys Ser Lys Arg Phe Val Glu Ser Leu Ser Asn 20 25 <210> 293 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 293 His Ser Gln Gly Thr Phe Thr Ser Asp Tyr Ser Lys Tyr Leu Asp Ser 1 5 10 15 Arg Arg Ala Gln Gln Phe Leu Lys Trp Leu Leu Asn 20 25 <210> 294 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 294 His Ser Gln Gly Thr Phe Thr Ser Asp Tyr Ser Lys His Leu Asp Ser 1 5 10 15 Arg Tyr Ala Gln Glu Phe Val Gln Trp Leu Met Asn 20 25 <210> 295 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 295 His Ser Glu Gly Thr Phe Ser Asn Asp Tyr Ser Lys Tyr Leu Glu Asp 1 5 10 15 Arg Lys Ala Gln Glu Phe Val Arg Trp Leu Met Asn 20 25 <210> 296 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 296 His Thr Asp Gly Ile Phe Ser Ser Asp Tyr Ser Lys Tyr Leu Asp Asn 1 5 10 15 Arg Arg Thr Lys Asp Phe Val Gln Trp Leu Leu Ser 20 25 <210> 297 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 297 His Ser Glu Gly Thr Phe Ser Ser Asp Tyr Ser Lys Tyr Leu Asp Ser 1 5 10 15 Arg Arg Ala Lys Asp Phe Val Gln Trp Leu Met Ser 20 25 <210> 298 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 298 Tyr Ala Glu Gly Thr Phe Ile Ser Asp Tyr Ser Ile Ala Met Asp Lys 1 5 10 15 Ile Arg Gln Gln Asp Phe Val Asn Trp Leu Leu Ala 20 25 <210> 299 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 299 His Ala Asp Gly Ile Phe Thr Thr Val Tyr Ser His Leu Leu Ala Lys 1 5 10 15 Leu Ala Val Lys Arg Tyr Leu His Ser Leu Ile Arg 20 25 <210> 300 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 300 His Ile Asp Gly Ile Phe Thr Asp Ser Tyr Ser Arg Tyr Arg Lys Gln 1 5 10 15 Met Ala Val Lys Lys Tyr Leu Ala Ala Val Leu Gly 20 25 <210> 301 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 301 His Ser Asp Ala Leu Phe Thr Asp Thr Tyr Thr Arg Leu Arg Lys Gln 1 5 10 15 Met Ala Met Lys Lys Tyr Leu Asn Ser Val Leu Asn 20 25 <210> 302 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 302 His Ser Asp Ala Val Phe Thr Asp Ser Tyr Thr Arg Leu Leu Lys Gln 1 5 10 15 Met Ala Met Arg Lys Tyr Leu Asp Ser Ile Leu Asn 20 25 <210> 303 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 303 His Ser Asp Ala Thr Phe Thr Ala Glu Tyr Ser Lys Leu Leu Ala Lys 1 5 10 15 Leu Ala Leu Gln Lys Tyr Leu Glu Ser Ile Leu Gly 20 25 <210> 304 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 304 Tyr Ala Asp Ala Ile Phe Thr Asn Ser Tyr Arg Lys Val Leu Gly Gln 1 5 10 15 Leu Ser Ala Arg Lys Leu Leu Gln Asp Ile Met Asn 20 25 <210> 305 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 305 His Ala Asp Ala Ile Phe Thr Ser Ser Tyr Arg Arg Ile Leu Gly Gln 1 5 10 15 Leu Tyr Ala Arg Lys Leu Leu His Glu Ile Met Asn 20 25 <210> 306 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 306 His Val Asp Ala Ile Phe Thr Thr Asn Tyr Arg Lys Leu Leu Ser Gln 1 5 10 15 Leu Tyr Ala Arg Lys Val Ile Gln Asp Ile Met Asn 20 25 <210> 307 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 307 Val Ala His Gly Ile Leu Asn Glu Ala Tyr Arg Lys Val Leu Asp Gln 1 5 10 15 Leu Ser Ala Gly Lys His Leu Gln Ser Leu Val Ala 20 25 <210> 308 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 308 Val Ala His Gly Ile Leu Asp Lys Ala Tyr Arg Lys Val Leu Asp Gln 1 5 10 15 Leu Ser Ala Arg Arg Tyr Leu Gln Thr Leu Met Ala 20 25 <210> 309 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 309 His Ala Asp Gly Met Phe Asn Lys Ala Tyr Arg Lys Ala Leu Gly Gln 1 5 10 15 Leu Ser Ala Arg Lys Tyr Leu His Ser Leu Met Ala 20 25 <210> 310 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 310 His Ala Asp Gly Ser Phe Ser Asp Glu Met Asn Thr Val Leu Asp Ser 1 5 10 15 Leu Ala Thr Arg Asp Phe Ile Asn Trp Leu Leu Gln 20 25 <210> 311 <211> 27 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 311 His Ser Asp Gly Thr Phe Thr Ser Glu Leu Ser Arg Leu Arg Glu Ser 1 5 10 15 Ala Arg Leu Gln Arg Leu Leu Gln Gly Leu Val 20 25 <210> 312 <211> 27 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 312 His Ser Asp Gly Leu Phe Thr Ser Glu Tyr Ser Lys Met Arg Gly Asn 1 5 10 15 Ala Gln Val Gln Lys Phe Ile Gln Asn Leu Met 20 25 <210> 313 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 313 His Ser Asp Gly Thr Phe Thr Ser Asp Leu Ser Lys Gln Met Glu Glu 1 5 10 15 Glu Ala Val Arg Leu Phe Ile Glu Trp Leu Lys Asn 20 25 <210> 314 <211> 31 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 314 His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Lys Gly Arg Gly 20 25 30 <210> 315 <211> 31 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 315 His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Lys Glu Phe Ile Ala Trp Leu Val Arg Gly Arg Gly 20 25 30 <210> 316 <211> 31 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 316 His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Lys Glu Phe Ile Ala Trp Leu Val Lys Gly Lys Gly 20 25 30 <210> 317 <211> 31 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 317 His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Lys Gly 20 25 30 <210> 318 <211> 32 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 318 His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Lys Gly Arg 20 25 30 <210> 319 <211> 33 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 319 His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Arg Gly Arg 20 25 30 Lys <210> 320 <211> 34 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 320 His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Arg Gly Arg 20 25 30 Arg Lys <210> 321 <211> 31 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 321 His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Lys Gly Lys Gly 20 25 30 <210> 322 <211> 31 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 322 His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Lys Glu Phe Ile Ala Trp Leu Val Arg Gly Lys Gly 20 25 30 <210> 323 <211> 33 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 323 His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Lys Gly Arg Gly Arg 20 25 30 Lys <210> 324 <211> 34 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 324 His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Lys Glu Phe Ile Ala Trp Leu Val Arg Gly Arg Gly Arg 20 25 30 Arg Lys <210> 325 <211> 33 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 325 His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Lys Gly Arg 20 25 30 Lys <210> 326 <211> 34 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 326 His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Lys Gly Arg 20 25 30 Arg Lys <210> 327 <211> 31 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 327 His Gly Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Lys Gly Arg Gly 20 25 30 <210> 328 <211> 31 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 328 His Gly Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Lys Glu Phe Ile Ala Trp Leu Val Arg Gly Arg Gly 20 25 30 <210> 329 <211> 31 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 329 His Gly Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Lys Glu Phe Ile Ala Trp Leu Val Lys Gly Lys Gly 20 25 30 <210> 330 <211> 31 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 330 His Gly Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Lys Gly 20 25 30 <210> 331 <211> 33 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 331 His Gly Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Arg Gly Arg 20 25 30 Lys <210> 332 <211> 34 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 332 His Gly Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Arg Gly Arg 20 25 30 Arg Lys <210> 333 <211> 31 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 333 His Gly Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Lys Gly Lys Gly 20 25 30 <210> 334 <211> 31 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 334 His Gly Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Lys Glu Phe Ile Ala Trp Leu Val Arg Gly Lys Gly 20 25 30 <210> 335 <211> 33 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 335 His Gly Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Lys Gly Arg Gly Arg 20 25 30 Lys <210> 336 <211> 34 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 336 His Gly Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Lys Glu Phe Ile Ala Trp Leu Val Arg Gly Arg Gly Arg 20 25 30 Arg Lys <210> 337 <211> 33 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 337 His Gly Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Lys Gly Arg 20 25 30 Lys <210> 338 <211> 34 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 338 His Gly Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Lys Gly Arg 20 25 30 Arg Lys <210> 339 <211> 32 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 339 His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Arg Gly Lys 20 25 30 <210> 340 <211> 33 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 340 His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Arg Gly Arg 20 25 30 Lys <210> 341 <211> 34 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 341 His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Arg Gly Arg 20 25 30 Arg Lys <210> 342 <211> 35 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 342 His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Arg Gly Arg 20 25 30 Arg Glu Lys 35 <210> 343 <211> 36 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 343 His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Arg Gly Arg 20 25 30 Arg Glu Phe Lys 35 <210> 344 <211> 37 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 344 His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Arg Gly Arg 20 25 30 Arg Glu Phe Pro Lys 35 <210> 345 <211> 38 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 345 His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Arg Gly Arg 20 25 30 Arg Glu Phe Pro Glu Lys 35 <210> 346 <211> 39 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 346 His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Arg Gly Arg 20 25 30 Arg Glu Phe Pro Glu Glu Lys 35 <210> 347 <211> 38 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 347 His Asp Glu Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val 1 5 10 15 Ser Ser Tyr Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu 20 25 30 Val Arg Gly Arg Gly Lys 35 <210> 348 <211> 39 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 348 His Asp Glu Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val 1 5 10 15 Ser Ser Tyr Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu 20 25 30 Val Arg Gly Arg Gly Arg Lys 35 <210> 349 <211> 40 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 349 His Asp Glu Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val 1 5 10 15 Ser Ser Tyr Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu 20 25 30 Val Arg Gly Arg Gly Arg Arg Lys 35 40 <210> 350 <211> 41 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 350 His Asp Glu Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val 1 5 10 15 Ser Ser Tyr Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu 20 25 30 Val Arg Gly Arg Gly Arg Arg Glu Lys 35 40 <210> 351 <211> 42 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 351 His Asp Glu Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val 1 5 10 15 Ser Ser Tyr Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu 20 25 30 Val Arg Gly Arg Gly Arg Arg Glu Phe Lys 35 40 <210> 352 <211> 43 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 352 His Asp Glu Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val 1 5 10 15 Ser Ser Tyr Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu 20 25 30 Val Arg Gly Arg Gly Arg Arg Glu Phe Pro Lys 35 40 <210> 353 <211> 44 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 353 His Asp Glu Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val 1 5 10 15 Ser Ser Tyr Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu 20 25 30 Val Arg Gly Arg Gly Arg Arg Glu Phe Pro Glu Lys 35 40 <210> 354 <211> 45 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 354 His Asp Glu Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val 1 5 10 15 Ser Ser Tyr Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu 20 25 30 Val Arg Gly Arg Gly Arg Arg Glu Phe Pro Glu Glu Lys 35 40 45 <210> 355 <211> 38 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 355 Asp Glu Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser 1 5 10 15 Ser Tyr Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val 20 25 30 Arg Gly Arg Gly Arg Lys 35 <210> 356 <211> 39 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 356 Asp Glu Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser 1 5 10 15 Ser Tyr Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val 20 25 30 Arg Gly Arg Gly Arg Arg Lys 35 <210> 357 <211> 40 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 357 Asp Glu Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser 1 5 10 15 Ser Tyr Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val 20 25 30 Arg Gly Arg Gly Arg Arg Glu Lys 35 40 <210> 358 <211> 41 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 358 Asp Glu Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser 1 5 10 15 Ser Tyr Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val 20 25 30 Arg Gly Arg Gly Arg Arg Glu Phe Lys 35 40 <210> 359 <211> 42 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 359 Asp Glu Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser 1 5 10 15 Ser Tyr Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val 20 25 30 Arg Gly Arg Gly Arg Arg Glu Phe Pro Lys 35 40 <210> 360 <211> 43 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 360 Asp Glu Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser 1 5 10 15 Ser Tyr Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val 20 25 30 Arg Gly Arg Gly Arg Arg Glu Phe Pro Glu Lys 35 40 <210> 361 <211> 44 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 361 Asp Glu Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser 1 5 10 15 Ser Tyr Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val 20 25 30 Arg Gly Arg Gly Arg Arg Glu Phe Pro Glu Glu Lys 35 40 <210> 362 <211> 36 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 362 Glu Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser 1 5 10 15 Tyr Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg 20 25 30 Gly Arg Gly Lys 35 <210> 363 <211> 37 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 363 Glu Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser 1 5 10 15 Tyr Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg 20 25 30 Gly Arg Gly Arg Lys 35 <210> 364 <211> 38 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 364 Glu Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser 1 5 10 15 Tyr Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg 20 25 30 Gly Arg Gly Arg Arg Lys 35 <210> 365 <211> 39 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 365 Glu Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser 1 5 10 15 Tyr Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg 20 25 30 Gly Arg Gly Arg Arg Glu Lys 35 <210> 366 <211> 40 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 366 Glu Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser 1 5 10 15 Tyr Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg 20 25 30 Gly Arg Gly Arg Arg Glu Phe Lys 35 40 <210> 367 <211> 41 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 367 Glu Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser 1 5 10 15 Tyr Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg 20 25 30 Gly Arg Gly Arg Arg Glu Phe Pro Lys 35 40 <210> 368 <211> 42 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 368 Glu Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser 1 5 10 15 Tyr Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg 20 25 30 Gly Arg Gly Arg Arg Glu Phe Pro Glu Lys 35 40 <210> 369 <211> 43 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 369 Glu Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser 1 5 10 15 Tyr Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg 20 25 30 Gly Arg Gly Arg Arg Glu Phe Pro Glu Glu Lys 35 40 <210> 370 <211> 35 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 370 Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr 1 5 10 15 Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly 20 25 30 Arg Gly Lys 35 <210> 371 <211> 36 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 371 Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr 1 5 10 15 Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly 20 25 30 Arg Gly Arg Lys 35 <210> 372 <211> 37 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 372 Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr 1 5 10 15 Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly 20 25 30 Arg Gly Arg Arg Lys 35 <210> 373 <211> 38 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 373 Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr 1 5 10 15 Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly 20 25 30 Arg Gly Arg Arg Glu Lys 35 <210> 374 <211> 39 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 374 Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr 1 5 10 15 Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly 20 25 30 Arg Gly Arg Arg Glu Phe Lys 35 <210> 375 <211> 40 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 375 Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr 1 5 10 15 Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly 20 25 30 Arg Gly Arg Arg Glu Phe Pro Lys 35 40 <210> 376 <211> 41 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 376 Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr 1 5 10 15 Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly 20 25 30 Arg Gly Arg Arg Glu Phe Pro Glu Lys 35 40 <210> 377 <211> 42 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 377 Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr 1 5 10 15 Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly 20 25 30 Arg Gly Arg Arg Glu Phe Pro Glu Glu Lys 35 40 <210> 378 <211> 34 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 378 Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu 1 5 10 15 Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Arg 20 25 30 Gly Lys <210> 379 <211> 35 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 379 Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu 1 5 10 15 Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Arg 20 25 30 Gly Arg Lys 35 <210> 380 <211> 36 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 380 Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu 1 5 10 15 Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Arg 20 25 30 Gly Arg Arg Lys 35 <210> 381 <211> 37 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 381 Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu 1 5 10 15 Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Arg 20 25 30 Gly Arg Arg Glu Lys 35 <210> 382 <211> 38 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 382 Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu 1 5 10 15 Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Arg 20 25 30 Gly Arg Arg Glu Phe Lys 35 <210> 383 <211> 39 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 383 Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu 1 5 10 15 Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Arg 20 25 30 Gly Arg Arg Glu Phe Pro Lys 35 <210> 384 <211> 40 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 384 Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu 1 5 10 15 Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Arg 20 25 30 Gly Arg Arg Glu Phe Pro Glu Lys 35 40 <210> 385 <211> 41 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 385 Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu 1 5 10 15 Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Arg 20 25 30 Gly Arg Arg Glu Phe Pro Glu Glu Lys 35 40 <210> 386 <211> 33 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 386 Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu 1 5 10 15 Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Arg Gly 20 25 30 Lys <210> 387 <211> 34 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 387 Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu 1 5 10 15 Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Arg Gly 20 25 30 Arg Lys <210> 388 <211> 35 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 388 Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu 1 5 10 15 Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Arg Gly 20 25 30 Arg Arg Lys 35 <210> 389 <211> 36 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 389 Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu 1 5 10 15 Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Arg Gly 20 25 30 Arg Arg Glu Lys 35 <210> 390 <211> 37 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 390 Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu 1 5 10 15 Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Arg Gly 20 25 30 Arg Arg Glu Phe Lys 35 <210> 391 <211> 38 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 391 Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu 1 5 10 15 Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Arg Gly 20 25 30 Arg Arg Glu Phe Pro Lys 35 <210> 392 <211> 39 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 392 Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu 1 5 10 15 Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Arg Gly 20 25 30 Arg Arg Glu Phe Pro Glu Lys 35 <210> 393 <211> 40 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 393 Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu 1 5 10 15 Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Arg Gly 20 25 30 Arg Arg Glu Phe Pro Glu Glu Lys 35 40 <210> 394 <211> 38 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 394 His Asp Glu Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val 1 5 10 15 Ser Ser Tyr Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu 20 25 30 Val Lys Gly Arg Gly Lys 35 <210> 395 <211> 38 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 395 His Asp Glu Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val 1 5 10 15 Ser Ser Tyr Leu Glu Gly Gln Ala Ala Lys Glu Phe Ile Ala Trp Leu 20 25 30 Val Arg Gly Arg Gly Lys 35 <210> 396 <211> 38 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 396 His Asp Glu Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val 1 5 10 15 Ser Ser Tyr Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu 20 25 30 Val Arg Gly Lys Gly Lys 35 <210> 397 <211> 32 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 397 His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Lys Gly Arg Gly Lys 20 25 30 <210> 398 <211> 32 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 398 His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Lys Glu Phe Ile Ala Trp Leu Val Arg Gly Arg Gly Lys 20 25 30 <210> 399 <211> 32 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 399 His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Lys Gly Lys 20 25 30 <210> 400 <211> 32 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 400 His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Arg Gly Lys 20 25 30 <210> 401 <211> 39 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 401 His Asp Glu Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val 1 5 10 15 Ser Ser Tyr Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu 20 25 30 Val Lys Gly Arg Gly Arg Lys 35 <210> 402 <211> 39 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 402 His Asp Glu Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val 1 5 10 15 Ser Ser Tyr Leu Glu Gly Gln Ala Ala Lys Glu Phe Ile Ala Trp Leu 20 25 30 Val Arg Gly Arg Gly Arg Lys 35 <210> 403 <211> 39 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 403 His Asp Glu Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val 1 5 10 15 Ser Ser Tyr Leu Glu Gly Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu 20 25 30 Val Arg Gly Lys Gly Arg Lys 35 <210> 404 <211> 33 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 404 His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Lys Gly Arg Gly Arg 20 25 30 Lys <210> 405 <211> 33 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 405 His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Lys Glu Phe Ile Ala Trp Leu Val Arg Gly Arg Gly Arg 20 25 30 Lys <210> 406 <211> 33 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 406 His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Lys Gly Arg 20 25 30 Lys <210> 407 <211> 32 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 407 His Gly Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Lys Gly Arg Gly Lys 20 25 30 <210> 408 <211> 32 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 408 His Gly Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 1 5 10 15 Gln Ala Ala Arg Glu Phe Ile Ala Trp Leu Val Arg Gly Lys Gly Lys 20 25 30 <210> 409 <211> 38 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 409 Phe Leu Phe His Tyr Ser Lys Thr Gln Lys Leu Gly Lys Ser Asn Val 1 5 10 15 Val Glu Glu Leu Gln Ser Pro Phe Ala Ser Gln Ser Arg Gly Tyr Phe 20 25 30 Leu Phe Arg Pro Arg Asn 35 <210> 410 <211> 177 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 410 Met Glu Ile Cys Arg Gly Leu Arg Ser His Leu Ile Thr Leu Leu Leu 1 5 10 15 Phe Leu Phe His Ser Glu Thr Ile Cys Arg Pro Ser Gly Arg Lys Ser 20 25 30 Ser Lys Met Gln Ala Phe Arg Ile Trp Asp Val Asn Gln Lys Thr Phe 35 40 45 Tyr Leu Arg Asn Asn Gln Leu Val Ala Gly Tyr Leu Gln Gly Pro Asn 50 55 60 Val Asn Leu Glu Glu Lys Ile Asp Val Val Pro Ile Glu Pro His Ala 65 70 75 80 Leu Phe Leu Gly Ile His Gly Gly Lys Met Cys Leu Ser Cys Val Lys 85 90 95 Ser Gly Asp Glu Thr Arg Leu Gln Leu Glu Ala Val Asn Ile Thr Asp 100 105 110 Leu Ser Glu Asn Arg Lys Gln Asp Lys Arg Phe Ala Phe Ile Arg Ser 115 120 125 Asp Ser Gly Pro Thr Thr Ser Phe Glu Ser Ala Ala Cys Pro Gly Trp 130 135 140 Phe Leu Cys Thr Ala Met Glu Ala Asp Gln Pro Val Ser Leu Thr Asn 145 150 155 160 Met Pro Asp Glu Gly Val Met Val Thr Lys Phe Tyr Phe Gln Glu Asp 165 170 175 Glu <210> 411 <211> 175 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 411 Met Glu Thr Cys Arg Cys Pro Leu Ser Tyr Leu Ile Ser Phe Leu Leu 1 5 10 15 Phe Leu Pro His Ser Glu Thr Ala Cys Arg Leu Gly Lys Arg Pro Cys 20 25 30 Arg Met Gln Ala Phe Arg Ile Trp Asp Val Asn Gln Lys Thr Phe Tyr 35 40 45 Leu Arg Asn Asn Gln Leu Val Ala Gly Tyr Leu Gln Gly Ser Asn Thr 50 55 60 Lys Leu Glu Glu Lys Leu Asp Val Val Pro Val Glu Pro His Ala Val 65 70 75 80 Phe Leu Gly Ile His Gly Gly Lys Leu Cys Leu Ala Cys Val Lys Ser 85 90 95 Gly Asp Glu Thr Arg Leu Gln Leu Glu Ala Val Asn Ile Thr Asp Leu 100 105 110 Ser Lys Asn Lys Asp Gln Asp Lys Arg Phe Thr Phe Ile Leu Ser Asp 115 120 125 Ser Gly Pro Thr Thr Ser Phe Glu Ser Ala Ala Cys Pro Gly Trp Phe 130 135 140 Leu Cys Thr Ala Leu Glu Ala Asp Arg Pro Val Ser Leu Thr Asn Arg 145 150 155 160 Pro Glu Glu Ala Met Met Val Thr Lys Phe Tyr Phe Gln Lys Glu 165 170 175 <210> 412 <211> 176 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 412 Met Arg Pro Ser Arg Ser Thr Arg Arg His Leu Ile Ser Leu Leu Leu 1 5 10 15 Phe Leu Phe His Ser Glu Thr Ala Cys Arg Pro Ser Gly Lys Arg Pro 20 25 30 Cys Arg Met Gln Ala Phe Arg Ile Trp Asp Val Asn Gln Lys Thr Phe 35 40 45 Tyr Leu Arg Asn Asn Gln Leu Val Ala Gly Tyr Leu Gln Gly Pro Asn 50 55 60 Ala Lys Leu Glu Glu Arg Ile Asp Val Val Pro Leu Glu Pro Gln Leu 65 70 75 80 Leu Phe Leu Gly Ile Gln Arg Gly Lys Leu Cys Leu Ser Cys Val Lys 85 90 95 Ser Gly Asp Lys Met Lys Leu His Leu Glu Ala Val Asn Ile Thr Asp 100 105 110 Leu Gly Lys Asn Lys Glu Gln Asp Lys Arg Phe Thr Phe Ile Arg Ser 115 120 125 Asn Ser Gly Pro Thr Thr Thr Phe Glu Ser Ala Ser Cys Pro Gly Trp 130 135 140 Phe Leu Cys Thr Ala Leu Glu Ala Asp Gln Pro Val Ser Leu Thr Asn 145 150 155 160 Thr Pro Asp Asp Ser Ile Val Val Thr Lys Phe Tyr Phe Gln Glu Asp 165 170 175 <210> 413 <211> 178 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 413 Met Glu Ile Cys Arg Gly Pro Tyr Ser His Leu Ile Ser Leu Leu Leu 1 5 10 15 Ile Leu Leu Phe Arg Ser Glu Ser Ala Gly His Ile Pro Ala Gly Lys 20 25 30 Arg Pro Cys Lys Met Gln Ala Phe Arg Ile Trp Asp Thr Asn Gln Lys 35 40 45 Thr Phe Tyr Leu Arg Asn Asn Gln Leu Ile Ala Gly Tyr Leu Gln Gly 50 55 60 Pro Asn Thr Lys Leu Glu Glu Lys Ile Asp Met Val Pro Ile Asp Phe 65 70 75 80 Arg Asn Val Phe Leu Gly Ile His Gly Gly Lys Leu Cys Leu Ser Cys 85 90 95 Val Lys Ser Gly Asp Asp Thr Lys Leu Gln Leu Glu Glu Val Asn Ile 100 105 110 Thr Asp Leu Asn Lys Asn Lys Glu Glu Asp Lys Arg Phe Thr Phe Ile 115 120 125 Arg Ser Glu Thr Gly Pro Thr Thr Ser Phe Glu Ser Leu Ala Cys Pro 130 135 140 Gly Trp Phe Leu Cys Thr Thr Leu Glu Ala Asp His Pro Val Ser Leu 145 150 155 160 Thr Asn Thr Pro Lys Glu Pro Cys Thr Val Thr Lys Phe Tyr Phe Gln 165 170 175 Glu Asp <210> 414 <211> 178 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 414 Met Glu Ile Cys Trp Gly Pro Tyr Ser His Leu Ile Ser Leu Leu Leu 1 5 10 15 Ile Leu Leu Phe His Ser Glu Ala Ala Cys Arg Pro Ser Gly Lys Arg 20 25 30 Pro Cys Lys Met Gln Ala Phe Arg Ile Trp Asp Thr Asn Gln Lys Thr 35 40 45 Phe Tyr Leu Arg Asn Asn Gln Leu Ile Ala Gly Tyr Leu Gln Gly Pro 50 55 60 Asn Ile Lys Leu Glu Glu Lys Ile Asp Met Val Pro Ile Asp Leu His 65 70 75 80 Ser Val Phe Leu Gly Ile His Gly Gly Lys Leu Cys Leu Ser Cys Ala 85 90 95 Lys Ser Gly Asp Asp Ile Lys Leu Gln Leu Glu Glu Val Asn Ile Thr 100 105 110 Asp Leu Ser Lys Asn Lys Glu Glu Asp Lys Arg Phe Thr Phe Ile Arg 115 120 125 Ser Glu Lys Gly Pro Thr Thr Ser Phe Glu Ser Ala Ala Cys Pro Gly 130 135 140 Trp Phe Leu Cys Thr Thr Leu Glu Ala Asp Arg Pro Val Ser Leu Thr 145 150 155 160 Asn Thr Pro Glu Glu Pro Leu Ile Val Thr Lys Phe Tyr Phe Gln Glu 165 170 175 Asp-Gln <210> 415 <211> 153 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 415 Met Arg Pro Ser Gly Arg Lys Ser Ser Lys Met Gln Ala Phe Arg Ile 1 5 10 15 Trp Asp Val Asn Gln Lys Thr Phe Tyr Leu Arg Asn Asn Gln Leu Val 20 25 30 Ala Gly Tyr Leu Gln Gly Pro Asn Val Asn Leu Glu Glu Lys Ile Asp 35 40 45 Val Val Pro Ile Glu Pro His Ala Leu Phe Leu Gly Ile His Gly Gly 50 55 60 Lys Met Cys Leu Ser Cys Val Lys Ser Gly Asp Glu Thr Arg Leu Gln 65 70 75 80 Leu Glu Ala Val Asn Ile Thr Asp Leu Ser Glu Asn Arg Lys Gln Asp 85 90 95 Lys Arg Phe Ala Phe Ile Arg Ser Asp Ser Gly Pro Thr Thr Ser Phe 100 105 110 Glu Ser Ala Ala Cys Pro Gly Trp Phe Leu Cys Thr Ala Met Glu Ala 115 120 125 Asp Gln Pro Val Ser Leu Thr Asn Met Pro Asp Glu Gly Val Met Val 130 135 140 Thr Lys Phe Tyr Phe Gln Glu Asp Glu 145 150 <210> 416 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 416 Ser Leu Arg Arg Ser Ser Cys Phe Gly Gly Arg Met Asp Arg Ile Gly 1 5 10 15 Ala Gln Ser Gly Leu Gly Cys Asn Ser Phe Arg Tyr 20 25 <210> 417 <211> 32 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 417 Ser Pro Lys Met Val Gln Gly Ser Gly Gly Phe Gly Arg Lys Met Asp 1 5 10 15 Arg Ile Ser Ser Ser Ser Gly Leu Gly Cys Lys Val Leu Arg Arg His 20 25 30 <210> 418 <211> 32 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 418 Asn Ser Lys Met Ala His Ser Ser Ser Cys Phe Gly Gln Lys Ile Asp 1 5 10 15 Arg Ile Gly Ala Val Ser Arg Leu Gly Cys Asp Gly Leu Arg Leu Phe 20 25 30 <210> 419 <211> 22 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 419 Gly Leu Ser Lys Gly Cys Phe Gly Leu Lys Leu Asp Arg Ile Gly Ser 1 5 10 15 Met Ser Gly Leu Gly Cys 20 <210> 420 <211> 146 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 420 Pro Ala Leu Pro Glu Asp Gly Gly Ser Gly Ala Phe Pro Pro Gly His 1 5 10 15 Phe Lys Asp Pro Lys Arg Leu Tyr Cys Lys Asn Gly Gly Phe Phe Leu 20 25 30 Arg Ile His Pro Asp Gly Arg Val Asp Gly Val Arg Glu Lys Ser Asp 35 40 45 Pro His Ile Lys Leu Gln Leu Gln Ala Glu Glu Arg Gly Val Val Ser 50 55 60 Ile Lys Gly Val Cys Ala Asn Arg Tyr Leu Ala Met Lys Glu Asp Gly 65 70 75 80 Arg Leu Leu Ala Ser Lys Cys Val Thr Asp Glu Cys Phe Phe Phe Glu 85 90 95 Arg Leu Glu Ser Asn Asn Tyr Asn Thr Tyr Arg Ser Arg Lys Tyr Thr 100 105 110 Ser Trp Tyr Val Ala Leu Lys Arg Thr Gly Gln Tyr Lys Leu Gly Ser 115 120 125 Lys Thr Gly Pro Gly Gln Lys Ala Ile Leu Phe Leu Pro Met Ser Ala 130 135 140 Lys Ser 145 <210> 421 <211> 235 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 421 Leu Pro Ala Gln Val Ala Phe Thr Pro Tyr Ala Pro Glu Pro Gly Ser 1 5 10 15 Thr Cys Arg Leu Arg Glu Tyr Tyr Asp Gln Thr Ala Gln Met Cys Cys 20 25 30 Ser Lys Cys Ser Pro Gly Gln His Ala Lys Val Phe Cys Thr Lys Thr 35 40 45 Ser Asp Thr Val Cys Asp Ser Cys Glu Asp Ser Thr Tyr Thr Gln Leu 50 55 60 Trp Asn Trp Val Pro Glu Cys Leu Ser Cys Gly Ser Arg Cys Ser Ser 65 70 75 80 Asp Gln Val Glu Thr Gln Ala Cys Thr Arg Glu Gln Asn Arg Ile Cys 85 90 95 Thr Cys Arg Pro Gly Trp Tyr Cys Ala Leu Ser Lys Gln Glu Gly Cys 100 105 110 Arg Leu Cys Ala Pro Leu Arg Lys Cys Arg Pro Gly Phe Gly Val Ala 115 120 125 Arg Pro Gly Thr Glu Thr Ser Asp Val Val Cys Lys Pro Cys Ala Pro 130 135 140 Gly Thr Phe Ser Asn Thr Thr Ser Ser Thr Asp Ile Cys Arg Pro His 145 150 155 160 Gln Ile Cys Asn Val Val Ala Ile Pro Gly Asn Ala Ser Met Asp Ala 165 170 175 Val Cys Thr Ser Thr Ser Pro Thr Arg Ser Met Ala Pro Gly Ala Val 180 185 190 His Leu Pro Gln Pro Val Ser Thr Arg Ser Gln His Thr Gln Pro Thr 195 200 205 Pro Glu Pro Ser Thr Ala Pro Ser Thr Ser Phe Leu Leu Pro Met Gly 210 215 220 Pro Ser Pro Pro Ala Glu Gly Ser Thr Gly Asp 225 230 235 <210> 422 <211> 191 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 422 Phe Pro Thr Ile Pro Leu Ser Arg Leu Phe Asp Asn Ala Met Leu Arg 1 5 10 15 Ala His Arg Leu His Gln Leu Ala Phe Asp Thr Tyr Gln Glu Phe Glu 20 25 30 Glu Ala Tyr Ile Pro Lys Glu Gln Lys Tyr Ser Phe Leu Gln Asn Pro 35 40 45 Gln Thr Ser Leu Cys Phe Ser Glu Ser Ile Pro Thr Pro Ser Asn Arg 50 55 60 Glu Glu Thr Gln Gln Lys Ser Asn Leu Glu Leu Leu Arg Ile Ser Leu 65 70 75 80 Leu Leu Ile Gln Ser Trp Leu Glu Pro Val Gln Phe Leu Arg Ser Val 85 90 95 Phe Ala Asn Ser Leu Val Tyr Gly Ala Ser Asp Ser Asn Val Tyr Asp 100 105 110 Leu Leu Lys Asp Leu Glu Glu Gly Ile Gln Thr Leu Met Gly Arg Leu 115 120 125 Glu Asp Gly Ser Pro Arg Thr Gly Gln Ile Phe Lys Gln Thr Tyr Ser 130 135 140 Lys Phe Asp Thr Asn Ser His Asn Asp Asp Ala Leu Leu Lys Asn Tyr 145 150 155 160 Gly Leu Leu Tyr Cys Phe Arg Lys Asp Met Asp Lys Val Glu Thr Phe 165 170 175 Leu Arg Ile Val Gln Cys Arg Ser Val Glu Gly Ser Cys Gly Phe 180 185 190 <210> 423 <211> 190 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 423 Phe Pro Ala Met Pro Leu Ser Ser Leu Phe Ala Asn Ala Val Leu Arg 1 5 10 15 Ala Gln His Leu His Gln Leu Ala Ala Asp Thr Tyr Lys Glu Phe Glu 20 25 30 Arg Ala Tyr Ile Pro Glu Gly Gln Arg Tyr Ser Ile Gln Asn Ala Gln 35 40 45 Ala Ala Phe Cys Phe Ser Glu Thr Ile Pro Ala Pro Thr Gly Lys Asp 50 55 60 Glu Ala Gln Gln Arg Ser Asp Val Glu Leu Leu Arg Phe Ser Leu Leu 65 70 75 80 Leu Ile Gln Ser Trp Leu Gly Pro Val Gln Phe Leu Ser Arg Val Phe 85 90 95 Thr Asn Ser Leu Val Phe Gly Thr Ser Asp Arg Val Tyr Glu Lys Leu 100 105 110 Lys Asp Leu Glu Glu Gly Ile Gln Ala Leu Met Arg Glu Leu Glu Asp 115 120 125 Gly Ser Pro Arg Ala Gly Gln Ile Leu Lys Gln Thr Tyr Asp Lys Phe 130 135 140 Asp Thr Asn Leu Arg Ser Asp Asp Ala Leu Leu Lys Asn Tyr Gly Leu 145 150 155 160 Leu Ser Cys Phe Lys Lys Asp Leu His Lys Ala Glu Thr Tyr Leu Arg 165 170 175 Val Met Lys Cys Arg Arg Phe Val Glu Ser Ser Cys Ala Phe 180 185 190 <210> 424 <211> 190 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 424 Phe Pro Ala Met Pro Leu Ser Ser Leu Phe Ala Asn Ala Val Leu Arg 1 5 10 15 Ala Gln His Leu His Gln Leu Ala Ala Asp Thr Tyr Lys Glu Phe Glu 20 25 30 Arg Thr Tyr Ile Pro Glu Gly Gln Arg Tyr Ser Ile Gln Asn Ala Gln 35 40 45 Ala Ala Phe Cys Phe Ser Glu Thr Ile Pro Ala Pro Thr Gly Lys Asp 50 55 60 Glu Ala Gln Gln Arg Ser Asp Val Glu Leu Leu Arg Phe Ser Leu Leu 65 70 75 80 Leu Ile Gln Ser Trp Leu Gly Pro Val Gln Phe Leu Ser Arg Val Phe 85 90 95 Thr Asn Ser Leu Val Phe Gly Thr Ser Asp Arg Val Tyr Glu Lys Leu 100 105 110 Lys Asp Leu Glu Glu Gly Ile Gln Ala Leu Met Arg Glu Leu Glu Asp 115 120 125 Gly Ser Pro Arg Ala Gly Gln Ile Leu Arg Gln Thr Tyr Asp Lys Phe 130 135 140 Asp Thr Asn Leu Arg Ser Asp Asp Ala Leu Leu Lys Asn Tyr Gly Leu 145 150 155 160 Leu Ser Cys Phe Lys Lys Asp Leu His Lys Ala Glu Thr Tyr Leu Arg 165 170 175 Val Met Lys Cys Arg Arg Phe Val Glu Ser Ser Cys Ala Phe 180 185 190 <210> 425 <211> 190 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 425 Phe Pro Ala Met Pro Leu Ser Ser Leu Phe Ala Asn Ala Val Leu Arg 1 5 10 15 Ala Gln His Leu His Gln Leu Ala Ala Asp Thr Tyr Lys Glu Phe Glu 20 25 30 Arg Thr Tyr Ile Pro Glu Gly Gln Arg Tyr Ser Ile Gln Asn Ala Gln 35 40 45 Ala Ala Phe Cys Phe Ser Glu Thr Ile Pro Ala Pro Thr Gly Lys Asp 50 55 60 Glu Ala Gln Gln Arg Ser Asp Val Glu Leu Leu Arg Phe Ser Leu Leu 65 70 75 80 Leu Ile Gln Ser Trp Leu Gly Pro Val Gln Phe Leu Ser Arg Val Phe 85 90 95 Thr Asn Ser Leu Val Phe Gly Thr Ser Asp Arg Val Tyr Glu Lys Leu 100 105 110 Lys Asp Leu Glu Glu Gly Ile Gln Ala Leu Met Arg Glu Leu Glu Asp 115 120 125 Gly Ser Pro Arg Ala Gly Gln Ile Leu Arg Gln Thr Tyr Asp Lys Phe 130 135 140 Asp Thr Asn Leu Arg Ser Asp Asp Ala Leu Leu Lys Asn Tyr Gly Leu 145 150 155 160 Leu Ser Cys Phe Lys Lys Asp Leu His Lys Ala Glu Thr Tyr Leu Arg 165 170 175 Val Met Lys Cys Arg Arg Phe Val Glu Ser Ser Cys Ala Phe 180 185 190 <210> 426 <211> 190 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 426 Phe Pro Ala Met Pro Leu Ser Ser Leu Phe Ala Asn Ala Val Leu Arg 1 5 10 15 Ala Gln His Leu His Gln Leu Ala Ala Asp Thr Tyr Lys Glu Phe Glu 20 25 30 Arg Ala Tyr Ile Pro Glu Gly Gln Arg Tyr Ser Ile Gln Asn Ala Gln 35 40 45 Ala Ala Phe Cys Phe Ser Glu Thr Ile Pro Ala Pro Thr Gly Lys Asp 50 55 60 Glu Ala Gln Gln Arg Ser Asp Met Glu Leu Leu Arg Phe Ser Leu Leu 65 70 75 80 Leu Ile Gln Ser Trp Leu Gly Pro Val Gln Leu Leu Ser Arg Val Phe 85 90 95 Thr Asn Ser Leu Val Phe Gly Thr Ser Asp Arg Val Tyr Glu Lys Leu 100 105 110 Arg Asp Leu Glu Glu Gly Ile Gln Ala Leu Met Arg Glu Leu Glu Asp 115 120 125 Gly Ser Pro Arg Ala Gly Gln Ile Leu Lys Gln Thr Tyr Asp Lys Phe 130 135 140 Asp Thr Asn Leu Arg Ser Asp Asp Ala Leu Leu Lys Asn Tyr Gly Leu 145 150 155 160 Leu Ser Cys Phe Lys Lys Asp Leu His Lys Ala Glu Thr Tyr Leu Arg 165 170 175 Val Met Lys Cys Arg Arg Phe Val Glu Ser Ser Cys Ala Phe 180 185 190 <210> 427 <211> 190 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 427 Phe Pro Ala Met Pro Leu Ser Ser Leu Phe Ala Asn Ala Val Leu Arg 1 5 10 15 Ala Gln His Leu His Gln Leu Ala Ala Asp Thr Tyr Lys Glu Phe Glu 20 25 30 Arg Ala Tyr Ile Pro Glu Gly Gln Arg Tyr Ser Ile Gln Asn Ala Gln 35 40 45 Ala Ala Phe Cys Phe Ser Glu Thr Ile Pro Ala Pro Thr Gly Lys Asp 50 55 60 Glu Ala Gln Gln Arg Ser Asp Val Glu Leu Leu Arg Phe Ser Leu Leu 65 70 75 80 Leu Ile Gln Ser Trp Leu Gly Pro Val Gln Phe Leu Ser Arg Val Phe 85 90 95 Thr Asn Ser Leu Val Phe Gly Thr Ser Asp Arg Val Tyr Glu Lys Leu 100 105 110 Lys Asp Leu Glu Glu Gly Ile Gln Ala Leu Met Arg Glu Leu Glu Asp 115 120 125 Gly Ser Pro Arg Pro Gly Gln Val Leu Lys Gln Thr Tyr Asp Lys Phe 130 135 140 Asp Thr Asn Met Arg Ser Asp Asp Ala Leu Leu Lys Asn Tyr Gly Leu 145 150 155 160 Leu Ser Cys Phe Lys Lys Asp Leu His Lys Ala Glu Thr Tyr Leu Arg 165 170 175 Val Met Lys Cys Arg Arg Phe Val Glu Ser Ser Cys Ala Phe 180 185 190 <210> 428 <211> 190 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 428 Phe Pro Ala Met Pro Leu Ser Ser Leu Phe Ala Asn Ala Val Leu Arg 1 5 10 15 Ala Gln His Leu His Gln Leu Ala Ala Asp Thr Tyr Lys Glu Phe Glu 20 25 30 Arg Ala Tyr Ile Pro Glu Gly Gln Arg Tyr Ser Ile Gln Asn Ala Gln 35 40 45 Ala Ala Phe Cys Phe Ser Glu Thr Ile Pro Ala Pro Thr Gly Lys Asp 50 55 60 Glu Ala Gln Gln Arg Ser Asp Val Glu Leu Leu Arg Phe Ser Leu Val 65 70 75 80 Leu Ile Gln Ser Trp Leu Gly Pro Leu Gln Phe Leu Ser Arg Val Phe 85 90 95 Thr Asn Ser Leu Val Phe Gly Thr Ser Asp Arg Val Tyr Glu Lys Leu 100 105 110 Lys Asp Leu Glu Glu Gly Ile Gln Ala Leu Met Arg Glu Leu Glu Asp 115 120 125 Gly Ser Pro Arg Ala Gly Gln Ile Leu Lys Gln Thr Tyr Asp Lys Phe 130 135 140 Asp Thr Asn Leu Arg Ser Asp Asp Ala Leu Leu Lys Asn Tyr Gly Leu 145 150 155 160 Leu Ser Cys Phe Lys Lys Asp Leu His Lys Ala Glu Thr Tyr Leu Arg 165 170 175 Val Met Lys Cys Arg Arg Phe Val Glu Ser Ser Cys Ala Phe 180 185 190 <210> 429 <211> 190 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 429 Phe Pro Ala Met Pro Leu Ser Ser Leu Phe Ala Asn Ala Val Leu Arg 1 5 10 15 Ala Gln His Leu His Gln Leu Ala Ala Asp Thr Tyr Lys Glu Phe Glu 20 25 30 Arg Ala Tyr Ile Pro Glu Gly Gln Arg Tyr Ser Ile Gln Asn Ala Gln 35 40 45 Ala Ala Phe Cys Phe Ser Glu Thr Ile Pro Ala Pro Thr Gly Lys Asp 50 55 60 Glu Ala Gln Gln Arg Ser Asp Val Glu Leu Leu Arg Phe Ser Leu Leu 65 70 75 80 Leu Ile Gln Ser Trp Leu Gly Pro Val Gln Phe Leu Ser Arg Val Phe 85 90 95 Thr Asn Ser Leu Val Phe Gly Thr Ser Asp Arg Val Tyr Glu Lys Leu 100 105 110 Lys Asp Leu Glu Glu Gly Ile Gln Ala Leu Met Arg Glu Leu Glu Asp 115 120 125 Gly Ser Pro Arg Ala Gly Gln Ile Leu Lys Gln Thr Tyr Asp Lys Phe 130 135 140 Asp Thr Asn Leu Arg Ser Asp Asp Ala Leu Leu Lys Asn Tyr Gly Leu 145 150 155 160 Leu Ser Cys Phe Lys Lys Asp Leu His Lys Ala Glu Thr Tyr Leu Arg 165 170 175 Val Met Lys Cys Arg Arg Phe Val Glu Ser Ser Cys Ala Phe 180 185 190 <210> 430 <211> 190 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 430 Phe Pro Ala Met Pro Leu Ser Ser Leu Phe Ala Asn Ala Val Leu Arg 1 5 10 15 Ala Gln His Leu His Gln Leu Ala Ala Asp Thr Tyr Lys Glu Phe Glu 20 25 30 Arg Ala Tyr Ile Pro Glu Gly Gln Arg Tyr Ser Ile Gln Asn Ala Gln 35 40 45 Ala Ala Phe Cys Phe Ser Glu Thr Ile Pro Ala Pro Thr Gly Lys Asp 50 55 60 Glu Ala Gln Gln Arg Ser Asp Val Glu Leu Leu Arg Phe Ser Leu Leu 65 70 75 80 Leu Ile Gln Ser Trp Leu Gly Pro Val Gln Phe Leu Ser Arg Val Phe 85 90 95 Thr Asn Ser Leu Val Phe Gly Thr Ser Asp Arg Val Tyr Glu Lys Leu 100 105 110 Lys Asp Leu Glu Glu Gly Ile Gln Ala Leu Met Arg Glu Leu Glu Asp 115 120 125 Gly Ser Pro Arg Gly Gly Gln Ile Leu Lys Gln Thr Tyr Asp Lys Phe 130 135 140 Asp Thr Asn Leu Arg Ser Asp Asp Ala Leu Leu Lys Asn Tyr Gly Leu 145 150 155 160 Leu Ser Cys Phe Lys Lys Asp Leu His Lys Ala Glu Thr Tyr Leu Arg 165 170 175 Val Met Lys Cys Arg Arg Phe Val Glu Ser Ser Cys Ala Phe 180 185 190 <210> 431 <211> 190 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 431 Phe Pro Ala Met Pro Leu Ser Ser Leu Phe Ala Asn Ala Val Leu Arg 1 5 10 15 Ala Gln His Leu His Gln Leu Ala Ala Asp Thr Tyr Lys Asp Phe Glu 20 25 30 Arg Ala Tyr Ile Pro Glu Gly Gln Arg Tyr Ser Ile Gln Asn Ala Gln 35 40 45 Ala Ala Phe Cys Phe Ser Glu Thr Ile Pro Ala Pro Thr Gly Lys Asp 50 55 60 Glu Ala Gln Gln Arg Ser Asp Met Glu Leu Leu Arg Phe Ser Leu Leu 65 70 75 80 Leu Ile Gln Ser Trp Leu Gly Pro Val Gln Phe Leu Ser Arg Val Phe 85 90 95 Thr Asn Ser Leu Val Phe Gly Thr Ser Asp Arg Val Tyr Glu Lys Leu 100 105 110 Lys Asp Leu Glu Glu Gly Ile Gln Ala Leu Met Arg Glu Leu Glu Asp 115 120 125 Gly Ser Pro Arg Ala Gly Pro Ile Leu Lys Gln Thr Tyr Asp Lys Phe 130 135 140 Asp Thr Asn Leu Arg Ser Asp Asp Ala Leu Leu Lys Asn Tyr Gly Leu 145 150 155 160 Leu Ser Cys Phe Lys Lys Asp Leu His Lys Ala Glu Thr Tyr Leu Arg 165 170 175 Val Met Lys Cys Arg Arg Phe Val Glu Ser Ser Cys Ala Phe 180 185 190 <210> 432 <211> 190 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 432 Phe Pro Ala Met Pro Leu Ser Ser Leu Phe Ala Asn Ala Val Leu Arg 1 5 10 15 Ala Gln His Leu His Gln Leu Ala Ala Asp Thr Tyr Lys Glu Phe Glu 20 25 30 Arg Ala Tyr Ile Pro Glu Gly Gln Arg Tyr Ser Ile Gln Asn Ala Gln 35 40 45 Ala Ala Phe Cys Phe Ser Glu Thr Ile Pro Ala Pro Thr Gly Lys Asp 50 55 60 Glu Ala Gln Gln Arg Ser Asp Val Glu Leu Leu Arg Phe Ser Leu Leu 65 70 75 80 Leu Ile Gln Ser Trp Leu Gly Pro Val Gln Phe Leu Ser Arg Val Phe 85 90 95 Thr Asn Ser Leu Val Phe Gly Thr Ser Asp Arg Val Tyr Glu Lys Leu 100 105 110 Lys Asp Leu Glu Glu Gly Ile Gln Ala Leu Met Arg Glu Leu Glu Asp 115 120 125 Gly Ser Pro Arg Ala Gly Gln Ile Leu Lys Gln Thr Tyr Asp Lys Phe 130 135 140 Asp Thr Asn Met Arg Ser Asp Asp Ala Leu Leu Lys Asn Tyr Gly Leu 145 150 155 160 Leu Ser Cys Phe Lys Lys Asp Leu His Lys Ala Glu Thr Tyr Leu Arg 165 170 175 Val Met Lys Cys Arg Arg Phe Val Glu Ser Ser Cys Ala Phe 180 185 190 <210> 433 <211> 190 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 433 Phe Pro Ala Met Pro Leu Ser Ser Leu Phe Ala Asn Ala Val Leu Arg 1 5 10 15 Ala Gln His Leu His Gln Leu Ala Ala Asp Thr Tyr Lys Glu Phe Glu 20 25 30 Arg Ala Tyr Ile Pro Glu Gly Gln Arg Tyr Ser Ile Gln Asn Thr Gln 35 40 45 Ala Ala Phe Cys Phe Ser Glu Thr Ile Pro Ala Pro Thr Gly Lys Asp 50 55 60 Glu Ala Gln Gln Arg Ser Asp Val Glu Leu Leu Arg Phe Ser Leu Leu 65 70 75 80 Leu Ile Gln Ser Trp Leu Gly Pro Val Gln Phe Leu Ser Arg Val Phe 85 90 95 Thr Asn Ser Leu Val Phe Gly Thr Ser Asp Arg Val Tyr Glu Lys Leu 100 105 110 Lys Asp Leu Glu Glu Gly Ile Gln Ala Leu Met Arg Glu Leu Glu Asp 115 120 125 Gly Ser Pro Arg Ala Gly Gln Ile Leu Lys Gln Thr Tyr Asp Lys Phe 130 135 140 Asp Thr Asn Met Arg Ser Asp Asp Ala Leu Leu Lys Asn Tyr Gly Leu 145 150 155 160 Leu Ser Cys Phe Lys Lys Asp Leu His Lys Ala Glu Thr Tyr Leu Arg 165 170 175 Val Met Lys Cys Arg Arg Phe Val Glu Ser Ser Cys Ala Phe 180 185 190 <210> 434 <211> 190 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 434 Phe Pro Ala Met Pro Leu Ser Ser Leu Phe Ala Asn Ala Val Leu Arg 1 5 10 15 Ala Gln His Leu His Gln Leu Ala Ala Asp Thr Tyr Lys Glu Phe Glu 20 25 30 Arg Ala Tyr Ile Pro Glu Gly Gln Arg Tyr Ser Ile Gln Asn Thr Gln 35 40 45 Ala Ala Phe Cys Phe Ser Glu Thr Ile Pro Ala Pro Thr Gly Lys Asp 50 55 60 Glu Ala Gln Gln Arg Ser Asp Val Glu Leu Leu Arg Phe Ser Leu Leu 65 70 75 80 Leu Ile Gln Ser Trp Leu Gly Pro Val Gln Phe Leu Ser Arg Val Phe 85 90 95 Thr Asn Ser Leu Val Phe Gly Thr Ser Asp Arg Val Tyr Glu Lys Leu 100 105 110 Lys Asp Leu Glu Glu Gly Ile Gln Ala Leu Met Arg Glu Leu Glu Asp 115 120 125 Gly Ser Pro Arg Ala Gly Gln Ile Leu Lys Gln Thr Tyr Asp Lys Phe 130 135 140 Asp Thr Asn Met Arg Ser Asp Asp Ala Leu Leu Lys Asn Tyr Gly Leu 145 150 155 160 Leu Ser Cys Phe Lys Lys Asp Leu His Lys Ala Glu Thr Tyr Leu Arg 165 170 175 Val Met Lys Cys Arg Arg Phe Val Glu Ser Ser Cys Ala Phe 180 185 190 <210> 435 <211> 190 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 435 Phe Pro Ala Met Pro Leu Ser Ser Leu Phe Ala Asn Ala Val Leu Arg 1 5 10 15 Ala Gln His Leu His Gln Leu Ala Ala Asp Thr Tyr Lys Glu Phe Glu 20 25 30 Arg Ala Tyr Ile Pro Glu Gly Gln Arg Tyr Ser Ile Gln Asn Ala Gln 35 40 45 Ala Ala Phe Cys Phe Ser Glu Thr Ile Pro Ala Pro Thr Gly Lys Asp 50 55 60 Glu Ala Gln Gln Arg Ser Asp Met Glu Leu Leu Arg Phe Ser Leu Leu 65 70 75 80 Leu Ile Gln Ser Trp Leu Gly Pro Val Gln Phe Leu Ser Arg Ala Phe 85 90 95 Thr Asn Thr Leu Val Phe Gly Thr Ser Asp Arg Val Tyr Glu Lys Leu 100 105 110 Lys Asp Leu Glu Glu Gly Ile Gln Ala Leu Met Arg Glu Leu Glu Asp 115 120 125 Gly Ser Pro Arg Val Gly Gln Leu Leu Lys Gln Thr Tyr Asp Lys Phe 130 135 140 Asp Thr Asn Leu Arg Gly Asp Asp Ala Leu Leu Lys Asn Tyr Gly Leu 145 150 155 160 Leu Ser Cys Phe Lys Lys Asp Leu His Lys Ala Glu Thr Tyr Leu Arg 165 170 175 Val Met Lys Cys Arg Arg Phe Val Glu Ser Ser Cys Val Phe 180 185 190 <210> 436 <211> 190 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 436 Phe Pro Ala Met Pro Leu Ser Ser Leu Phe Ala Asn Ala Val Leu Arg 1 5 10 15 Ala Gln His Leu His Gln Leu Ala Ala Asp Thr Tyr Lys Glu Phe Glu 20 25 30 Arg Ala Tyr Ile Pro Glu Gly Gln Arg Tyr Ser Ile Gln Asn Ala Gln 35 40 45 Ala Ala Phe Cys Phe Ser Glu Thr Ile Pro Ala Pro Thr Gly Lys Glu 50 55 60 Glu Ala Gln Gln Arg Thr Asp Met Glu Leu Leu Arg Phe Ser Leu Leu 65 70 75 80 Leu Ile Gln Ser Trp Leu Gly Pro Val Gln Phe Leu Ser Arg Ile Phe 85 90 95 Thr Asn Ser Leu Met Phe Gly Thr Ser Asp Arg Val Tyr Glu Lys Leu 100 105 110 Lys Asp Leu Glu Glu Gly Ile Gln Ala Leu Met Gln Glu Leu Glu Asp 115 120 125 Gly Ser Pro Arg Ile Gly Gln Ile Leu Lys Gln Thr Tyr Asp Lys Phe 130 135 140 Asp Ala Asn Met Arg Ser Asp Asp Ala Leu Leu Lys Asn Tyr Gly Leu 145 150 155 160 Leu Ser Cys Phe Lys Lys Asp Leu His Lys Ala Glu Thr Tyr Leu Arg 165 170 175 Val Met Lys Cys Arg Arg Phe Ala Glu Ser Ser Cys Ala Phe 180 185 190 <210> 437 <211> 190 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 437 Phe Pro Ala Met Pro Leu Ser Ser Leu Phe Ser Asn Ala Val Leu Arg 1 5 10 15 Ala Gln His Leu His Gln Leu Ala Ala Asp Thr Tyr Lys Glu Phe Glu 20 25 30 Arg Ala Tyr Ile Pro Glu Gly Gln Arg Tyr Ser Ile Gln Asn Ala Gln 35 40 45 Ala Ala Phe Cys Phe Ser Glu Thr Ile Pro Ala Pro Thr Gly Lys Glu 50 55 60 Glu Ala Gln Gln Arg Thr Asp Met Glu Leu Leu Arg Phe Ser Leu Leu 65 70 75 80 Leu Ile Gln Ser Trp Leu Gly Pro Val Gln Phe Leu Ser Arg Ile Phe 85 90 95 Thr Asn Ser Leu Met Phe Gly Thr Ser Asp Arg Val Tyr Glu Lys Leu 100 105 110 Lys Asp Leu Glu Glu Gly Ile Gln Ala Leu Met Gln Glu Leu Glu Asp 115 120 125 Gly Ser Pro Arg Val Gly Gln Ile Leu Lys Gln Thr Tyr Asp Lys Phe 130 135 140 Asp Ala Asn Met Arg Ser Asp Asp Ala Leu Leu Lys Asn Tyr Gly Leu 145 150 155 160 Leu Ser Cys Phe Lys Lys Asp Leu His Lys Ala Glu Thr Tyr Leu Arg 165 170 175 Val Met Lys Cys Arg Arg Phe Val Glu Ser Ser Cys Ala Phe 180 185 190 <210> 438 <211> 190 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 438 Phe Pro Ala Met Pro Leu Ser Ser Leu Phe Ala Asn Ala Val Leu Arg 1 5 10 15 Ala Gln His Leu His Gln Leu Ala Ala Asp Thr Tyr Lys Glu Phe Glu 20 25 30 Arg Ala Tyr Ile Pro Glu Gly Gln Arg Tyr Ser Ile Gln Asn Ala Gln 35 40 45 Thr Ala Phe Cys Phe Ser Glu Thr Ile Pro Ala Pro Thr Gly Lys Glu 50 55 60 Glu Ala Gln Gln Arg Ser Asp Met Glu Leu Leu Arg Phe Ser Leu Leu 65 70 75 80 Leu Ile Gln Ser Trp Leu Gly Pro Val Gln Phe Leu Ser Arg Ile Phe 85 90 95 Thr Asn Ser Leu Met Phe Gly Thr Ser Asp Arg Val Tyr Glu Lys Leu 100 105 110 Lys Asp Leu Glu Glu Gly Ile Gln Ala Leu Met Gln Glu Leu Glu Asp 115 120 125 Gly Ser Pro Arg Val Gly Gln Ile Leu Lys Gln Thr Tyr Asp Lys Phe 130 135 140 Asp Thr Asn Met Arg Ser Asp Asp Ala Leu Leu Lys Asn Tyr Gly Leu 145 150 155 160 Leu Ser Cys Phe Lys Lys Asp Leu His Lys Ala Glu Thr Tyr Leu Arg 165 170 175 Val Met Lys Cys Arg Arg Phe Val Glu Ser Ser Cys Ala Phe 180 185 190 <210> 439 <211> 190 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 439 Phe Pro Ala Met Pro Leu Ser Asn Leu Phe Ala Asn Ala Val Leu Arg 1 5 10 15 Ala Gln His Leu His Gln Leu Ala Ala Asp Thr Tyr Lys Glu Phe Glu 20 25 30 Arg Ala Tyr Ile Pro Glu Gly Gln Arg Tyr Ser Ile Gln Asn Ala Gln 35 40 45 Ala Ala Phe Cys Phe Ser Glu Thr Ile Pro Ala Pro Thr Gly Lys Glu 50 55 60 Glu Ala Gln Gln Arg Ser Asp Met Glu Leu Leu Arg Phe Ser Leu Leu 65 70 75 80 Leu Ile Gln Ser Trp Leu Gly Pro Val Gln Phe Leu Ser Arg Val Phe 85 90 95 Thr Asn Ser Leu Val Phe Gly Thr Ser Asp Arg Val Phe Glu Lys Leu 100 105 110 Lys Asp Leu Glu Glu Gly Ile Gln Ala Leu Met Arg Glu Leu Glu Asp 115 120 125 Gly Ser Leu Arg Ala Gly Gln Leu Leu Lys Gln Thr Tyr Asp Lys Phe 130 135 140 Asp Thr Asn Met Arg Ser Asp Asp Ala Leu Leu Lys Asn Tyr Gly Leu 145 150 155 160 Leu Ser Cys Phe Lys Lys Asp Leu His Lys Ala Glu Thr Tyr Leu Arg 165 170 175 Val Met Lys Cys Arg Arg Phe Val Glu Ser Ser Cys Ala Phe 180 185 190 <210> 440 <211> 190 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 440 Phe Pro Ala Met Pro Leu Ser Ser Leu Phe Gly Asn Ala Val Leu Arg 1 5 10 15 Ala Gln His Leu His Gln Leu Ala Ala Asp Thr Tyr Lys Glu Phe Glu 20 25 30 Arg Thr Tyr Ile Pro Glu Gly Gln Arg Tyr Ser Ile His Asn Thr Gln 35 40 45 Thr Ala Phe Cys Phe Ser Glu Thr Ile Pro Ala Pro Thr Asp Lys Glu 50 55 60 Glu Ala Gln Gln Arg Ser Asp Val Glu Leu Leu His Phe Ser Leu Leu 65 70 75 80 Leu Ile Gln Ser Trp Leu Gly Pro Val Gln Phe Leu Ser Arg Val Phe 85 90 95 Thr Asn Ser Leu Val Phe Gly Thr Ser Asp Arg Val Tyr Glu Lys Leu 100 105 110 Lys Asp Leu Glu Glu Gly Ile Gln Ala Leu Met Arg Glu Leu Glu Asp 115 120 125 Gly Thr Pro Arg Ala Gly Gln Ile Leu Lys Gln Thr Tyr Asp Lys Phe 130 135 140 Asp Thr Asn Leu Arg Ser Asn Asp Ala Leu Leu Lys Asn Tyr Gly Leu 145 150 155 160 Leu Ser Cys Phe Arg Lys Asp Leu His Arg Thr Glu Thr Tyr Leu Arg 165 170 175 Val Met Lys Cys Arg Arg Phe Val Glu Ser Ser Cys Ala Phe 180 185 190 <210> 441 <211> 191 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 441 Ala Phe Pro Ala Met Ser Leu Ser Gly Leu Phe Ala Asn Ala Val Leu 1 5 10 15 Arg Ala Gln His Leu His Gln Leu Ala Ala Asp Thr Phe Lys Glu Phe 20 25 30 Glu Arg Thr Tyr Ile Pro Glu Gly Gln Arg Tyr Ser Ile Gln Asn Thr 35 40 45 Gln Val Ala Phe Cys Phe Ser Glu Thr Ile Pro Ala Pro Thr Gly Lys 50 55 60 Asn Glu Ala Gln Gln Lys Ser Asp Leu Glu Leu Leu Arg Ile Ser Leu 65 70 75 80 Leu Leu Ile Gln Ser Trp Leu Gly Pro Leu Gln Phe Leu Ser Arg Val 85 90 95 Phe Thr Asn Ser Leu Val Phe Gly Thr Ser Asp Arg Val Tyr Glu Lys 100 105 110 Leu Lys Asp Leu Glu Glu Gly Ile Leu Ala Leu Met Arg Glu Leu Glu 115 120 125 Asp Gly Thr Pro Arg Ala Gly Gln Ile Leu Lys Gln Thr Tyr Asp Lys 130 135 140 Phe Asp Thr Asn Met Arg Ser Asp Asp Ala Leu Leu Lys Asn Tyr Gly 145 150 155 160 Leu Leu Ser Cys Phe Arg Lys Asp Leu His Lys Thr Glu Thr Tyr Leu 165 170 175 Arg Val Met Lys Cys Arg Arg Phe Gly Glu Ala Ser Cys Ala Phe 180 185 190 <210> 442 <211> 191 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 442 Ala Phe Pro Ala Met Ser Leu Ser Gly Leu Phe Ala Asn Ala Val Leu 1 5 10 15 Arg Ala Gln His Leu His Gln Leu Ala Ala Asp Thr Phe Lys Glu Phe 20 25 30 Glu Arg Thr Tyr Ile Pro Glu Gly Gln Arg Tyr Ser Ile Gln Asn Thr 35 40 45 Gln Val Ala Phe Cys Phe Ser Glu Thr Ile Pro Ala Pro Thr Gly Lys 50 55 60 Asn Glu Ala Gln Gln Lys Ser Asp Leu Glu Leu Leu Arg Ile Ser Leu 65 70 75 80 Leu Leu Ile Gln Ser Trp Leu Gly Pro Leu Gln Phe Leu Ser Arg Val 85 90 95 Phe Thr Asn Ser Leu Val Phe Gly Thr Ser Asp Arg Val Tyr Glu Lys 100 105 110 Leu Lys Asp Leu Glu Glu Gly Ile Leu Ala Leu Met Arg Glu Leu Glu 115 120 125 Asp Val Thr Pro Arg Ala Gly Gln Ile Leu Lys Gln Thr Tyr Asp Lys 130 135 140 Phe Asp Thr Asn Met Arg Ser Asp Asp Ala Leu Leu Lys Asn Tyr Gly 145 150 155 160 Leu Leu Ser Cys Phe Arg Lys Asp Leu His Lys Thr Glu Thr Tyr Leu 165 170 175 Arg Val Met Lys Cys Arg Arg Phe Gly Glu Ala Ser Cys Ala Phe 180 185 190 <210> 443 <211> 190 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 443 Phe Pro Ala Met Ser Leu Ser Gly Leu Phe Ala Asn Ala Val Leu Arg 1 5 10 15 Ala Gln His Leu His Gln Leu Ala Ala Asp Thr Phe Lys Glu Phe Glu 20 25 30 Arg Thr Tyr Ile Pro Glu Gly Gln Arg Tyr Ser Ile Gln Asn Thr Gln 35 40 45 Val Ala Phe Cys Phe Ser Glu Thr Ile Pro Ala Pro Thr Gly Lys Asn 50 55 60 Glu Ala Gln Gln Lys Ser Asp Leu Glu Leu Leu Arg Ile Ser Leu Leu 65 70 75 80 Leu Ile Gln Ser Trp Leu Gly Pro Leu Gln Phe Leu Ser Arg Val Phe 85 90 95 Thr Asn Ser Leu Val Phe Gly Thr Ser Asp Arg Val Tyr Glu Lys Leu 100 105 110 Lys Asp Leu Glu Glu Gly Ile Leu Ala Leu Met Arg Glu Leu Glu Asp 115 120 125 Gly Thr Pro Arg Ala Gly Gln Ile Leu Lys Gln Thr Tyr Asp Lys Phe 130 135 140 Asp Thr Asn Met Arg Ser Asp Asp Ala Leu Leu Lys Asn Tyr Gly Leu 145 150 155 160 Leu Ser Cys Phe Arg Lys Asp Leu His Lys Thr Glu Thr Tyr Leu Arg 165 170 175 Val Met Lys Cys Arg Arg Phe Gly Glu Ala Ser Cys Ala Phe 180 185 190 <210> 444 <211> 191 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 444 Ala Phe Pro Ala Met Ser Leu Ser Gly Leu Phe Ala Asn Ala Val Leu 1 5 10 15 Arg Ala Gln His Leu His Gln Leu Ala Ala Asp Thr Phe Lys Glu Phe 20 25 30 Glu Arg Thr Tyr Ile Pro Glu Gly Gln Arg Tyr Ser Ile Gln Asn Thr 35 40 45 Gln Val Ala Phe Cys Phe Ser Glu Thr Ile Pro Ala Pro Thr Gly Lys 50 55 60 Asn Glu Ala Gln Gln Lys Ser Asp Leu Glu Leu Leu Arg Ile Ser Leu 65 70 75 80 Leu Leu Ile Gln Ser Trp Leu Gly Pro Leu Gln Phe Leu Ser Arg Val 85 90 95 Phe Ser Asn Ser Leu Val Phe Gly Thr Ser Asp Arg Val Tyr Glu Lys 100 105 110 Leu Lys Asp Leu Glu Glu Gly Ile Leu Ala Leu Met Arg Glu Leu Glu 115 120 125 Asp Gly Thr Pro Arg Ala Gly Gln Ile Leu Lys Gln Thr Tyr Asp Lys 130 135 140 Phe Asp Thr Asn Met Arg Ser Asp Asp Ala Leu Leu Lys Asn Tyr Gly 145 150 155 160 Leu Leu Ser Cys Phe Arg Lys Asp Leu His Lys Thr Glu Thr Tyr Leu 165 170 175 Arg Val Met Lys Cys Arg Arg Phe Gly Glu Ala Ser Cys Ala Phe 180 185 190 <210> 445 <211> 190 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 445 Phe Pro Ala Met Ser Leu Ser Gly Leu Phe Ala Asn Ala Val Leu Arg 1 5 10 15 Val Gln His Leu His Gln Leu Ala Ala Asp Thr Phe Lys Glu Phe Glu 20 25 30 Arg Thr Tyr Ile Pro Glu Gly Gln Arg Tyr Ser Ile Gln Asn Thr Gln 35 40 45 Val Ala Phe Cys Phe Ser Glu Thr Ile Pro Ala Pro Thr Gly Lys Asn 50 55 60 Glu Ala Gln Gln Lys Ser Asp Leu Glu Leu Leu Arg Ile Ser Leu Leu 65 70 75 80 Leu Ile Gln Ser Trp Leu Gly Pro Leu Gln Phe Leu Ser Arg Val Phe 85 90 95 Thr Asn Ser Leu Val Phe Gly Thr Ser Asp Arg Val Tyr Glu Lys Leu 100 105 110 Lys Asp Leu Glu Glu Gly Ile Leu Ala Leu Met Arg Glu Leu Glu Asp 115 120 125 Gly Pro Pro Arg Ala Gly Gln Ile Leu Lys Gln Thr Tyr Asp Lys Phe 130 135 140 Asp Thr Asn Met Arg Ser Asp Asp Ala Leu Leu Lys Asn Tyr Gly Leu 145 150 155 160 Leu Ser Cys Phe Arg Lys Asp Leu His Lys Thr Glu Thr Tyr Leu Arg 165 170 175 Val Met Lys Cys Arg Arg Phe Gly Glu Ala Ser Cys Ala Phe 180 185 190 <210> 446 <211> 190 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 446 Phe Pro Ala Met Pro Leu Ser Ser Leu Phe Ala Asn Ala Val Leu Arg 1 5 10 15 Ala Gln His Leu His Gln Leu Ala Ala Asp Thr Tyr Lys Glu Phe Glu 20 25 30 Arg Ala Tyr Ile Pro Glu Gly Gln Arg Tyr Ser Ile Gln Asn Ala Gln 35 40 45 Ala Ala Phe Cys Phe Ser Glu Thr Ile Pro Ala Pro Thr Gly Lys Asp 50 55 60 Glu Ala Gln Gln Arg Ser Asp Met Glu Leu Leu Arg Phe Ser Leu Leu 65 70 75 80 Leu Ile Gln Ser Trp Leu Gly Pro Val Gln Leu Leu Ser Arg Val Phe 85 90 95 Thr Asn Ser Leu Val Leu Gly Thr Ser Asp Arg Val Tyr Glu Lys Leu 100 105 110 Lys Asp Leu Glu Glu Gly Ile Gln Ala Leu Met Arg Glu Leu Glu Asp 115 120 125 Gly Ser Pro Arg Val Gly Gln Ile Leu Lys Gln Thr Tyr Asp Lys Phe 130 135 140 Asp Thr Asn Leu Arg Ser Asp Asp Ala Leu Leu Lys Asn Tyr Gly Leu 145 150 155 160 Leu Ser Cys Phe Lys Lys Asp Leu His Lys Ala Glu Thr Tyr Leu Arg 165 170 175 Val Met Lys Cys Arg Arg Phe Val Glu Ser Ser Cys Ala Phe 180 185 190 <210> 447 <211> 191 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 447 Phe Pro Thr Ile Pro Leu Ser Arg Leu Leu Asp Asn Ala Met Leu Arg 1 5 10 15 Ala His Arg Leu His Gln Leu Ala Phe Asp Thr Tyr Gln Glu Phe Glu 20 25 30 Glu Ala Tyr Ile Pro Lys Glu Gln Lys Tyr Ser Phe Leu Gln Asn Pro 35 40 45 Gln Thr Ser Leu Cys Phe Ser Glu Ser Ile Pro Thr Pro Ala Ser Lys 50 55 60 Lys Glu Thr Gln Gln Lys Ser Asn Leu Glu Leu Leu Arg Met Ser Leu 65 70 75 80 Leu Leu Ile Gln Ser Trp Phe Glu Pro Val Gln Phe Leu Arg Ser Val 85 90 95 Phe Ala Asn Ser Leu Leu Tyr Gly Val Ser Asp Ser Asp Val Tyr Glu 100 105 110 Tyr Leu Lys Asp Leu Glu Glu Gly Ile Gln Thr Leu Met Gly Arg Leu 115 120 125 Glu Asp Gly Ser Pro Arg Thr Gly Glu Ile Phe Met Gln Thr Tyr Arg 130 135 140 Lys Phe Asp Val Asn Ser Gln Asn Asn Asp Ala Leu Leu Lys Asn Tyr 145 150 155 160 Gly Leu Leu Tyr Cys Phe Arg Lys Asp Met Asp Lys Val Glu Thr Phe 165 170 175 Leu Arg Ile Val Gln Cys Arg Ser Val Glu Gly Ser Cys Gly Phe 180 185 190 <210> 448 <211> 190 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 448 Phe Pro Ala Met Pro Leu Ser Ser Leu Phe Ala Asn Ala Val Leu Arg 1 5 10 15 Ala Gln His Leu His Gln Leu Val Ala Asp Thr Tyr Lys Glu Phe Glu 20 25 30 Arg Thr Tyr Ile Pro Glu Ala Gln Arg His Ser Ile Gln Ser Thr Gln 35 40 45 Thr Ala Phe Cys Phe Ser Glu Thr Ile Pro Ala Pro Thr Gly Lys Asp 50 55 60 Glu Ala Gln Gln Arg Ser Asp Val Glu Leu Leu Arg Phe Ser Leu Leu 65 70 75 80 Leu Ile Gln Ser Trp Leu Ser Pro Val Gln Phe Leu Ser Arg Val Phe 85 90 95 Thr Asn Ser Leu Val Phe Gly Thr Ser Asp Arg Val Tyr Glu Lys Leu 100 105 110 Arg Asp Leu Glu Glu Gly Ile Gln Ala Leu Met Gln Glu Leu Glu Asp 115 120 125 Gly Ser Ser Arg Gly Gly Leu Val Leu Lys Thr Thr Tyr Asp Lys Phe 130 135 140 Asp Thr Asn Leu Arg Ser Asp Glu Ala Leu Leu Lys Asn Tyr Gly Leu 145 150 155 160 Leu Ser Cys Phe Lys Lys Asp Leu His Lys Ala Glu Thr Tyr Leu Arg 165 170 175 Val Met Lys Cys Arg Arg Phe Val Glu Ser Ser Cys Ala Phe 180 185 190 <210> 449 <211> 191 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 449 Phe Pro Thr Ile Pro Leu Ser Arg Leu Phe Asp Asn Ala Met Leu Arg 1 5 10 15 Ala His Arg Leu His Gln Leu Ala Phe Asp Thr Tyr Gln Glu Phe Glu 20 25 30 Glu Ala Tyr Ile Pro Lys Glu Gln Lys Tyr Ser Phe Leu Gln Asn Pro 35 40 45 Gln Thr Ser Leu Cys Phe Ser Glu Ser Ile Pro Thr Pro Ser Asn Arg 50 55 60 Glu Glu Thr Gln Gln Lys Ser Asn Leu Glu Leu Leu Arg Ile Ser Leu 65 70 75 80 Leu Leu Ile Gln Ser Trp Leu Glu Pro Val Gln Phe Leu Arg Ser Val 85 90 95 Phe Ala Asn Ser Leu Val Tyr Gly Thr Ser Tyr Ser Asp Val Tyr Asp 100 105 110 Leu Leu Lys Asp Leu Glu Glu Gly Ile Gln Thr Leu Met Gly Arg Leu 115 120 125 Glu Asp Gly Ser Ser Arg Thr Gly Gln Ile Phe Lys Gln Thr Tyr Ser 130 135 140 Lys Phe Asp Thr Asn Ser His Asn Asn Asp Ala Leu Leu Lys Asn Tyr 145 150 155 160 Gly Leu Leu Tyr Cys Phe Arg Lys Asp Met Asp Lys Ile Glu Thr Phe 165 170 175 Leu Arg Ile Val Gln Cys Arg Ser Val Glu Gly Ser Cys Gly Phe 180 185 190 <210> 450 <211> 177 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 450 Met Glu Ile Cys Arg Gly Leu Arg Ser His Leu Ile Thr Leu Leu Leu 1 5 10 15 Phe Leu Phe His Ser Glu Thr Ile Cys Arg Pro Ser Gly Arg Lys Ser 20 25 30 Ser Lys Met Gln Ala Phe Arg Ile Trp Asp Val Asn Gln Lys Thr Phe 35 40 45 Tyr Leu Arg Asn Asn Gln Leu Val Ala Gly Tyr Leu Gln Gly Pro Asn 50 55 60 Val Asn Leu Glu Glu Lys Ile Asp Val Val Pro Ile Glu Pro His Ala 65 70 75 80 Leu Phe Leu Gly Ile His Gly Gly Lys Met Cys Leu Ser Cys Val Lys 85 90 95 Ser Gly Asp Glu Thr Arg Leu Gln Leu Glu Ala Val Asn Ile Thr Asp 100 105 110 Leu Ser Glu Asn Arg Lys Gln Asp Lys Arg Phe Ala Phe Ile Arg Ser 115 120 125 Asp Ser Gly Pro Thr Thr Ser Phe Glu Ser Ala Ala Cys Pro Gly Trp 130 135 140 Phe Leu Cys Thr Ala Met Glu Ala Asp Gln Pro Val Ser Leu Thr Asn 145 150 155 160 Met Pro Asp Glu Gly Val Met Val Thr Lys Phe Tyr Phe Gln Glu Asp 165 170 175 Glu <210> 451 <211> 175 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 451 Met Glu Thr Cys Arg Cys Pro Leu Ser Tyr Leu Ile Ser Phe Leu Leu 1 5 10 15 Phe Leu Pro His Ser Glu Thr Ala Cys Arg Leu Gly Lys Arg Pro Cys 20 25 30 Arg Met Gln Ala Phe Arg Ile Trp Asp Val Asn Gln Lys Thr Phe Tyr 35 40 45 Leu Arg Asn Asn Gln Leu Val Ala Gly Tyr Leu Gln Gly Ser Asn Thr 50 55 60 Lys Leu Glu Glu Lys Leu Asp Val Val Pro Val Glu Pro His Ala Val 65 70 75 80 Phe Leu Gly Ile His Gly Gly Lys Leu Cys Leu Ala Cys Val Lys Ser 85 90 95 Gly Asp Glu Thr Arg Leu Gln Leu Glu Ala Val Asn Ile Thr Asp Leu 100 105 110 Ser Lys Asn Lys Asp Gln Asp Lys Arg Phe Thr Phe Ile Leu Ser Asp 115 120 125 Ser Gly Pro Thr Thr Ser Phe Glu Ser Ala Ala Cys Pro Gly Trp Phe 130 135 140 Leu Cys Thr Ala Leu Glu Ala Asp Arg Pro Val Ser Leu Thr Asn Arg 145 150 155 160 Pro Glu Glu Ala Met Met Val Thr Lys Phe Tyr Phe Gln Lys Glu 165 170 175 <210> 452 <211> 176 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 452 Met Arg Pro Ser Arg Ser Thr Arg Arg His Leu Ile Ser Leu Leu Leu 1 5 10 15 Phe Leu Phe His Ser Glu Thr Ala Cys Arg Pro Ser Gly Lys Arg Pro 20 25 30 Cys Arg Met Gln Ala Phe Arg Ile Trp Asp Val Asn Gln Lys Thr Phe 35 40 45 Tyr Leu Arg Asn Asn Gln Leu Val Ala Gly Tyr Leu Gln Gly Pro Asn 50 55 60 Ala Lys Leu Glu Glu Arg Ile Asp Val Val Pro Leu Glu Pro Gln Leu 65 70 75 80 Leu Phe Leu Gly Ile Gln Arg Gly Lys Leu Cys Leu Ser Cys Val Lys 85 90 95 Ser Gly Asp Lys Met Lys Leu His Leu Glu Ala Val Asn Ile Thr Asp 100 105 110 Leu Gly Lys Asn Lys Glu Gln Asp Lys Arg Phe Thr Phe Ile Arg Ser 115 120 125 Asn Ser Gly Pro Thr Thr Thr Phe Glu Ser Ala Ser Cys Pro Gly Trp 130 135 140 Phe Leu Cys Thr Ala Leu Glu Ala Asp Gln Pro Val Ser Leu Thr Asn 145 150 155 160 Thr Pro Asp Asp Ser Ile Val Val Thr Lys Phe Tyr Phe Gln Glu Asp 165 170 175 <210> 453 <211> 178 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 453 Met Glu Ile Cys Arg Gly Pro Tyr Ser His Leu Ile Ser Leu Leu Leu 1 5 10 15 Ile Leu Leu Phe Arg Ser Glu Ser Ala Gly His Ile Pro Ala Gly Lys 20 25 30 Arg Pro Cys Lys Met Gln Ala Phe Arg Ile Trp Asp Thr Asn Gln Lys 35 40 45 Thr Phe Tyr Leu Arg Asn Asn Gln Leu Ile Ala Gly Tyr Leu Gln Gly 50 55 60 Pro Asn Thr Lys Leu Glu Glu Lys Ile Asp Met Val Pro Ile Asp Phe 65 70 75 80 Arg Asn Val Phe Leu Gly Ile His Gly Gly Lys Leu Cys Leu Ser Cys 85 90 95 Val Lys Ser Gly Asp Asp Thr Lys Leu Gln Leu Glu Glu Val Asn Ile 100 105 110 Thr Asp Leu Asn Lys Asn Lys Glu Glu Asp Lys Arg Phe Thr Phe Ile 115 120 125 Arg Ser Glu Thr Gly Pro Thr Thr Ser Phe Glu Ser Leu Ala Cys Pro 130 135 140 Gly Trp Phe Leu Cys Thr Thr Leu Glu Ala Asp His Pro Val Ser Leu 145 150 155 160 Thr Asn Thr Pro Lys Glu Pro Cys Thr Val Thr Lys Phe Tyr Phe Gln 165 170 175 Glu Asp <210> 454 <211> 178 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 454 Met Glu Ile Cys Trp Gly Pro Tyr Ser His Leu Ile Ser Leu Leu Leu 1 5 10 15 Ile Leu Leu Phe His Ser Glu Ala Ala Cys Arg Pro Ser Gly Lys Arg 20 25 30 Pro Cys Lys Met Gln Ala Phe Arg Ile Trp Asp Thr Asn Gln Lys Thr 35 40 45 Phe Tyr Leu Arg Asn Asn Gln Leu Ile Ala Gly Tyr Leu Gln Gly Pro 50 55 60 Asn Ile Lys Leu Glu Glu Lys Ile Asp Met Val Pro Ile Asp Leu His 65 70 75 80 Ser Val Phe Leu Gly Ile His Gly Gly Lys Leu Cys Leu Ser Cys Ala 85 90 95 Lys Ser Gly Asp Asp Ile Lys Leu Gln Leu Glu Glu Val Asn Ile Thr 100 105 110 Asp Leu Ser Lys Asn Lys Glu Glu Asp Lys Arg Phe Thr Phe Ile Arg 115 120 125 Ser Glu Lys Gly Pro Thr Thr Ser Phe Glu Ser Ala Ala Cys Pro Gly 130 135 140 Trp Phe Leu Cys Thr Thr Leu Glu Ala Asp Arg Pro Val Ser Leu Thr 145 150 155 160 Asn Thr Pro Glu Glu Pro Leu Ile Val Thr Lys Phe Tyr Phe Gln Glu 165 170 175 Asp-Gln <210> 455 <211> 153 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 455 Met Arg Pro Ser Gly Arg Lys Ser Ser Lys Met Gln Ala Phe Arg Ile 1 5 10 15 Trp Asp Val Asn Gln Lys Thr Phe Tyr Leu Arg Asn Asn Gln Leu Val 20 25 30 Ala Gly Tyr Leu Gln Gly Pro Asn Val Asn Leu Glu Glu Lys Ile Asp 35 40 45 Val Val Pro Ile Glu Pro His Ala Leu Phe Leu Gly Ile His Gly Gly 50 55 60 Lys Met Cys Leu Ser Cys Val Lys Ser Gly Asp Glu Thr Arg Leu Gln 65 70 75 80 Leu Glu Ala Val Asn Ile Thr Asp Leu Ser Glu Asn Arg Lys Gln Asp 85 90 95 Lys Arg Phe Ala Phe Ile Arg Ser Asp Ser Gly Pro Thr Thr Ser Phe 100 105 110 Glu Ser Ala Ala Cys Pro Gly Trp Phe Leu Cys Thr Ala Met Glu Ala 115 120 125 Asp Gln Pro Val Ser Leu Thr Asn Met Pro Asp Glu Gly Val Met Val 130 135 140 Thr Lys Phe Tyr Phe Gln Glu Asp Glu 145 150 <210> 456 <211> 178 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 456 Met His Ser Ser Ala Leu Leu Cys Cys Leu Val Leu Leu Thr Gly Val 1 5 10 15 Arg Ala Ser Pro Gly Gln Gly Thr Gln Ser Glu Asn Ser Cys Thr His 20 25 30 Phe Pro Gly Asn Leu Pro Asn Met Leu Arg Asp Leu Arg Asp Ala Phe 35 40 45 Ser Arg Val Lys Thr Phe Phe Gln Met Lys Asp Gln Leu Asp Asn Leu 50 55 60 Leu Leu Lys Glu Ser Leu Leu Glu Asp Phe Lys Gly Tyr Leu Gly Cys 65 70 75 80 Gln Ala Leu Ser Glu Met Ile Gln Phe Tyr Leu Glu Glu Val Met Pro 85 90 95 Gln Ala Glu Asn Gln Asp Pro Asp Ile Lys Ala His Val Asn Ser Leu 100 105 110 Gly Glu Asn Leu Lys Thr Leu Arg Leu Arg Leu Arg Arg Cys His Arg 115 120 125 Phe Leu Pro Cys Glu Asn Lys Ser Lys Ala Val Glu Gln Val Lys Asn 130 135 140 Ala Phe Asn Lys Leu Gln Glu Lys Gly Ile Tyr Lys Ala Met Ser Glu 145 150 155 160 Phe Asp Ile Phe Ile Asn Tyr Ile Glu Ala Tyr Met Thr Met Lys Ile 165 170 175 Arg Asn <210> 457 <211> 11 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 457 Tyr Gly Arg Lys Lys Arg Arg Gln Arg Arg Arg 1 5 10 <210> 458 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 458 Arg Arg Gln Arg Arg Thr Ser Lys Leu Met Lys Arg 1 5 10 <210> 459 <211> 27 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 459 Gly Trp Thr Leu Asn Ser Ala Gly Tyr Leu Leu Gly Lys Ile Asn Leu 1 5 10 15 Lys Ala Leu Ala Ala Leu Ala Lys Lys Ile Leu 20 25 <210> 460 <211> 33 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 460 Lys Ala Leu Ala Trp Glu Ala Lys Leu Ala Lys Ala Leu Ala Lys Ala 1 5 10 15 Leu Ala Lys His Leu Ala Lys Ala Leu Ala Lys Ala Leu Lys Cys Glu 20 25 30 Ala <210> 461 <211> 16 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 461 Arg Gln Ile Lys Ile Trp Phe Gln Asn Arg Arg Met Lys Trp Lys Lys 1 5 10 15 <210> 462 <211> 11 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 462 Tyr Gly Arg Lys Lys Arg Arg Gln Arg Arg Arg 1 5 10 <210> 463 <211> 9 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 463 Arg Lys Lys Arg Arg Gln Arg Arg Arg 1 5 <210> 464 <211> 11 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 464 Tyr Gly Arg Lys Lys Arg Arg Gln Arg Arg Arg 1 5 10 <210> 465 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 465 Arg Lys Lys Arg Arg Gln Arg Arg 1 5 <210> 466 <211> 11 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 466 Tyr Ala Arg Ala Ala Ala Arg Gln Ala Arg Ala 1 5 10 <210> 467 <211> 11 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 467 Thr His Arg Leu Pro Arg Arg Arg Arg Arg Arg 1 5 10 <210> 468 <211> 11 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 468 Gly Gly Arg Arg Ala Arg Arg Arg Arg Arg Arg 1 5 10 <210> 469 <211> 119 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 469 Gln Val Gln Leu Val Gln Ser Gly Gly Gly Val Val Gln Pro Gly Arg 1 5 10 15 Ser Leu Arg Leu Ser Cys Lys Ala Ser Gly Tyr Thr Phe Thr Arg Tyr 20 25 30 Thr Met His Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile 35 40 45 Gly Tyr Ile Asn Pro Ser Arg Gly Tyr Thr Asn Tyr Asn Gln Lys Val 50 55 60 Lys Asp Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Ala Phe 65 70 75 80 Leu Gln Met Asp Ser Leu Arg Pro Glu Asp Thr Gly Val Tyr Phe Cys 85 90 95 Ala Arg Tyr Tyr Asp Asp His Tyr Cys Leu Asp Tyr Trp Gly Gln Gly 100 105 110 Thr Pro Val Thr Val Ser Ser 115 <210> 470 <211> 122 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 470 Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Tyr Ser Phe Thr Gly Tyr 20 25 30 Thr Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ala Leu Ile Asn Pro Tyr Lys Gly Val Ser Thr Tyr Asn Gln Lys Phe 50 55 60 Lys Asp Arg Phe Thr Ile Ser Val Asp Lys Ser Lys Asn Thr Ala Tyr 65 70 75 80 Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Ser Gly Tyr Tyr Gly Asp Ser Asp Trp Tyr Phe Asp Val Trp 100 105 110 Gly Gln Gly Thr Leu Val Thr Val Ser Ser 115 120 <210> 471 <211> 119 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 471 Gln Val Gln Leu Val Gln Ser Gly Gly Gly Val Val Gln Pro Gly Arg 1 5 10 15 Ser Leu Arg Leu Ser Cys Lys Ala Ser Gly Tyr Thr Phe Thr Ser Tyr 20 25 30 Thr Met His Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile 35 40 45 Gly Tyr Ile Asn Pro Ser Ser Gly Tyr Thr Lys Tyr Asn Gln Lys Phe 50 55 60 Lys Asp Arg Phe Thr Ile Ser Ala Asp Lys Ser Lys Ser Thr Ala Phe 65 70 75 80 Leu Gln Met Asp Ser Leu Arg Pro Glu Asp Thr Gly Val Tyr Phe Cys 85 90 95 Ala Arg Trp Gln Asp Tyr Asp Val Tyr Phe Asp Tyr Trp Gly Gln Gly 100 105 110 Thr Pro Val Thr Val Ser Ser 115 <210> 472 <211> 119 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 472 Gln Val Gln Leu Gln Gln Ser Gly Ala Glu Leu Ala Arg Pro Gly Ala 1 5 10 15 Ser Val Lys Met Ser Cys Lys Ala Ser Gly Tyr Thr Phe Thr Arg Tyr 20 25 30 Thr Met His Trp Val Lys Gln Arg Pro Gly Gln Gly Leu Glu Trp Ile 35 40 45 Gly Tyr Ile Asn Pro Ser Arg Gly Tyr Thr Asn Tyr Asn Gln Lys Phe 50 55 60 Lys Asp Lys Ala Thr Leu Thr Thr Asp Lys Ser Ser Ser Thr Ala Tyr 65 70 75 80 Met Gln Leu Ser Ser Leu Thr Ser Glu Asp Ser Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Tyr Tyr Asp Asp His Tyr Cys Leu Asp Tyr Trp Gly Gln Gly 100 105 110 Thr Thr Leu Thr Val Ser Ser 115 <210> 473 <211> 119 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 473 Asp Ile Lys Leu Gln Gln Ser Gly Ala Glu Leu Ala Arg Pro Gly Ala 1 5 10 15 Ser Val Lys Met Ser Cys Lys Thr Ser Gly Tyr Thr Phe Thr Arg Tyr 20 25 30 Thr Met His Trp Val Lys Gln Arg Pro Gly Gln Gly Leu Glu Trp Ile 35 40 45 Gly Tyr Ile Asn Pro Ser Arg Gly Tyr Thr Asn Tyr Asn Gln Lys Phe 50 55 60 Lys Asp Lys Ala Thr Leu Thr Thr Asp Lys Ser Ser Ser Thr Ala Tyr 65 70 75 80 Met Gln Leu Ser Ser Leu Thr Ser Glu Asp Ser Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Tyr Tyr Asp Asp His Tyr Cys Leu Asp Tyr Trp Gly Gln Gly 100 105 110 Thr Thr Leu Thr Val Ser Ser 115 <210> 474 <211> 119 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 474 Asp Val Gln Leu Val Gln Ser Gly Ala Glu Val Lys Lys Pro Gly Ala 1 5 10 15 Ser Val Lys Val Ser Cys Lys Ala Ser Gly Tyr Thr Phe Thr Arg Tyr 20 25 30 Thr Met His Trp Val Arg Gln Ala Pro Gly Gln Gly Leu Glu Trp Ile 35 40 45 Gly Tyr Ile Asn Pro Ser Arg Gly Tyr Thr Asn Tyr Ala Asp Ser Val 50 55 60 Lys Gly Arg Phe Thr Ile Thr Thr Asp Lys Ser Thr Ser Thr Ala Tyr 65 70 75 80 Met Glu Leu Ser Ser Leu Arg Ser Glu Asp Thr Ala Thr Tyr Tyr Cys 85 90 95 Ala Arg Tyr Tyr Asp Asp His Tyr Cys Leu Asp Tyr Trp Gly Gln Gly 100 105 110 Thr Thr Val Thr Val Ser Ser 115 <210> 475 <211> 125 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 475 Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 1 5 10 15 Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Lys Tyr 20 25 30 Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp 50 55 60 Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr 65 70 75 80 Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr 85 90 95 Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Ile Ser Tyr Trp 100 105 110 Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 115 120 125 <210> 476 <211> 125 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 476 Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr 20 25 30 Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Gly Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp 50 55 60 Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr 65 70 75 80 Leu Tyr Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr 85 90 95 Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe 100 105 110 Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 115 120 125 <210> 477 <211> 125 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 477 Glu Val Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 1 5 10 15 Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr 20 25 30 Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp 50 55 60 Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr 65 70 75 80 Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr 85 90 95 Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe 100 105 110 Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 115 120 125 <210> 478 <211> 125 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 478 Glu Val Lys Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Lys Gly 1 5 10 15 Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr 20 25 30 Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp 50 55 60 Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Gln Ser Ile 65 70 75 80 Leu Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Met Tyr 85 90 95 Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe 100 105 110 Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 115 120 125 <210> 479 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 479 Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Ser Ala Ser Ser Ser Val Ser Tyr Met 20 25 30 Asn Trp Tyr Gln Gln Thr Pro Gly Lys Ala Pro Lys Arg Trp Ile Tyr 35 40 45 Asp Thr Ser Lys Leu Ala Ser Gly Val Pro Ser Arg Phe Ser Gly Ser 50 55 60 Gly Ser Gly Thr Asp Tyr Thr Phe Thr Ile Ser Ser Leu Gln Pro Glu 65 70 75 80 Asp Ile Ala Thr Tyr Tyr Cys Gln Gln Trp Ser Ser Asn Pro Phe Thr 85 90 95 Phe Gly Gln Gly Thr Lys Leu Gln Ile Thr Arg 100 105 <210> 480 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 480 Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Arg Ala Ser Gln Asp Ile Arg Asn Tyr 20 25 30 Leu Asn Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile 35 40 45 Tyr Tyr Thr Ser Arg Leu Glu Ser Gly Val Pro Ser Arg Phe Ser Gly 50 55 60 Ser Gly Ser Gly Thr Asp Tyr Thr Leu Thr Ile Ser Ser Leu Gln Pro 65 70 75 80 Glu Asp Phe Ala Thr Tyr Tyr Cys Gln Gln Gly Asn Thr Leu Pro Trp 85 90 95 Thr Phe Gly Gln Gly Thr Lys Val Glu Ile Lys 100 105 <210> 481 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 481 Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Met Thr Cys Arg Ala Ser Ser Ser Val Ser Tyr Met 20 25 30 His Trp Tyr Gln Gln Thr Pro Gly Lys Ala Pro Lys Pro Trp Ile Tyr 35 40 45 Ala Thr Ser Asn Leu Ala Ser Gly Val Pro Ser Arg Phe Ser Gly Ser 50 55 60 Gly Ser Gly Thr Asp Tyr Thr Leu Thr Ile Ser Ser Leu Gln Pro Glu 65 70 75 80 Asp Ile Ala Thr Tyr Tyr Cys Gln Gln Trp Ser Ser Asn Pro Pro Thr 85 90 95 Phe Gly Gln Gly Thr Lys Leu Gln Ile Thr Arg 100 105 <210> 482 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 482 Gln Ile Val Leu Thr Gln Ser Pro Ala Ile Met Ser Ala Ser Pro Gly 1 5 10 15 Glu Lys Val Thr Met Thr Cys Ser Ala Ser Ser Ser Val Ser Tyr Met 20 25 30 Asn Trp Tyr Gln Gln Lys Ser Gly Thr Ser Pro Lys Arg Trp Ile Tyr 35 40 45 Asp Thr Ser Lys Leu Ala Ser Gly Val Pro Ala His Phe Arg Gly Ser 50 55 60 Gly Ser Gly Thr Ser Tyr Ser Leu Thr Ile Ser Gly Met Glu Ala Glu 65 70 75 80 Asp Ala Ala Thr Tyr Tyr Cys Gln Gln Trp Ser Ser Asn Pro Phe Thr 85 90 95 Phe Gly Ser Gly Thr Lys Leu Glu Ile Asn Arg 100 105 <210> 483 <211> 106 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 483 Asp Ile Gln Leu Thr Gln Ser Pro Ala Ile Met Ser Ala Ser Pro Gly 1 5 10 15 Glu Lys Val Thr Met Thr Cys Arg Ala Ser Ser Ser Val Ser Tyr Met 20 25 30 Asn Trp Tyr Gln Gln Lys Ser Gly Thr Ser Pro Lys Arg Trp Ile Tyr 35 40 45 Asp Thr Ser Lys Val Ala Ser Gly Val Pro Tyr Arg Phe Ser Gly Ser 50 55 60 Gly Ser Gly Thr Ser Tyr Ser Leu Thr Ile Ser Ser Met Glu Ala Glu 65 70 75 80 Asp Ala Ala Thr Tyr Tyr Cys Gln Gln Trp Ser Ser Asn Pro Leu Thr 85 90 95 Phe Gly Ala Gly Thr Lys Leu Glu Leu Lys 100 105 <210> 484 <211> 106 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 484 Asp Ile Val Leu Thr Gln Ser Pro Ala Thr Leu Ser Leu Ser Pro Gly 1 5 10 15 Glu Arg Ala Thr Leu Ser Cys Arg Ala Ser Gln Ser Val Ser Tyr Met 20 25 30 Asn Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Arg Trp Ile Tyr 35 40 45 Asp Thr Ser Lys Val Ala Ser Gly Val Pro Ala Arg Phe Ser Gly Ser 50 55 60 Gly Ser Gly Thr Asp Tyr Ser Leu Thr Ile Asn Ser Leu Glu Ala Glu 65 70 75 80 Asp Ala Ala Thr Tyr Tyr Cys Gln Gln Trp Ser Ser Asn Pro Leu Thr 85 90 95 Phe Gly Gly Gly Thr Lys Val Glu Ile Lys 100 105 <210> 485 <211> 109 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 485 Gln Thr Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly 1 5 10 15 Thr Val Thr Leu Thr Cys Gly Ser Ser Thr Gly Ala Val Thr Ser Gly 20 25 30 Tyr Tyr Pro Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly 35 40 45 Leu Ile Gly Gly Thr Lys Phe Leu Ala Pro Gly Thr Pro Ala Arg Phe 50 55 60 Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val 65 70 75 80 Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Ala Leu Trp Tyr Ser Asn 85 90 95 Arg Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 100 105 <210> 486 <211> 109 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 486 Gln Ala Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly 1 5 10 15 Thr Val Thr Leu Thr Cys Gly Ser Ser Thr Gly Ala Val Thr Thr Ser 20 25 30 Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly 35 40 45 Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Val Pro Ala Arg Phe 50 55 60 Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Ala 65 70 75 80 Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Ala Leu Trp Tyr Ser Asn 85 90 95 Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 100 105 <210> 487 <211> 109 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 487 Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly 1 5 10 15 Thr Val Thr Leu Thr Cys Arg Ser Ser Thr Gly Ala Val Thr Thr Ser 20 25 30 Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly 35 40 45 Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr Pro Ala Arg Phe 50 55 60 Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val 65 70 75 80 Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Ala Leu Trp Tyr Ser Asn 85 90 95 Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 100 105 <210> 488 <211> 109 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 488 Gln Ala Val Val Thr Gln Glu Ser Ala Leu Thr Thr Ser Pro Gly Glu 1 5 10 15 Thr Val Thr Leu Thr Cys Arg Ser Ser Thr Gly Ala Val Thr Thr Ser 20 25 30 Asn Tyr Ala Asn Trp Val Gln Glu Lys Pro Asp His Leu Phe Thr Gly 35 40 45 Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Val Pro Ala Arg Phe 50 55 60 Ser Gly Ser Leu Ile Gly Asp Lys Ala Ala Leu Thr Ile Thr Gly Ala 65 70 75 80 Gln Thr Glu Asp Glu Ala Ile Tyr Phe Cys Ala Leu Trp Tyr Ser Asn 85 90 95 Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 100 105 <210> 489 <211> 11 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 489 Arg Ala Ser Gln Asp Ile Arg Asn Tyr Leu Asn 1 5 10 <210> 490 <211> 7 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 490 Tyr Thr Ser Arg Leu Glu Ser 1 5 <210> 491 <211> 9 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 491 Gln Gln Gly Asn Thr Leu Pro Trp Thr 1 5 <210> 492 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 492 Gly Tyr Ser Phe Thr Gly Tyr Thr Met Asn 1 5 10 <210> 493 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 493 Leu Ile Asn Pro Tyr Lys Gly Val Ser Thr 1 5 10 <210> 494 <211> 13 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 494 Ser Gly Tyr Tyr Gly Asp Ser Asp Trp Tyr Phe Asp Val 1 5 10 <210> 495 <211> 30 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 495 Gly Ser Gly Glu Gly Ser Glu Gly Glu Gly Gly Gly Glu Gly Ser Glu 1 5 10 15 Gly Glu Gly Ser Gly Glu Gly Gly Glu Gly Glu Gly Ser Gly 20 25 30 <210> 496 <211> 32 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 496 Thr Gly Ser Gly Glu Gly Ser Glu Gly Glu Gly Gly Gly Glu Gly Ser 1 5 10 15 Glu Gly Glu Gly Ser Gly Glu Gly Gly Glu Gly Glu Gly Ser Gly Thr 20 25 30 <210> 497 <211> 30 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 497 Gly Ala Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu 1 5 10 15 Thr Thr Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly 20 25 30 <210> 498 <211> 30 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 498 Gly Ser Ala Ala Pro Thr Ala Gly Thr Thr Pro Ser Ala Ser Pro Ala 1 5 10 15 Pro Pro Thr Gly Gly Ser Ser Ala Ala Gly Ser Pro Ser Thr 20 25 30 <210> 499 <211> 6 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 499 Ser Gly Gly Gly Gly Ser 1 5 <210> 500 <211> 5 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 500 Gly Gly Gly Gly Ser 1 5 <210> 501 <211> 6 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 501 Gly Gly Ser Gly Gly Ser 1 5 <210> 502 <211> 14 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 502 Arg Ser Ser Asn Gly Ala Val Thr Ser Ser Asn Tyr Ala Asn 1 5 10 <210> 503 <211> 14 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 503 Arg Ser Ser Asn Gly Glu Val Thr Thr Ser Asn Tyr Ala Asn 1 5 10 <210> 504 <211> 14 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 504 Arg Ser Ser Thr Gly Ala Val Thr Thr Ser Asn Tyr Ala Asn 1 5 10 <210> 505 <211> 7 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 505 Gly Thr Asn Lys Arg Ala Pro 1 5 <210> 506 <211> 7 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 506 Gly Thr Ile Lys Arg Ala Pro 1 5 <210> 507 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 507 Ala Leu Trp Tyr Pro Asn Leu Trp Val Phe 1 5 10 <210> 508 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 508 Ala Leu Trp Tyr Ser Asn Leu Trp Val Phe 1 5 10 <210> 509 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 509 Gly Phe Thr Phe Asn Thr Tyr Ala Met Asn 1 5 10 <210> 510 <211> 19 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 510 Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Ser 1 5 10 15 Val Lys Asp <210> 511 <211> 14 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 511 His Glu Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe Ala His 1 5 10 <210> 512 <211> 14 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 512 His Gly Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe Ala Tyr 1 5 10 <210> 513 <211> 22 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 513 Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly 1 5 10 15 Thr Val Thr Leu Thr Cys 20 <210> 514 <211> 15 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 514 Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly Leu Ile Gly 1 5 10 15 <210> 515 <211> 32 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 515 Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala 1 5 10 15 Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Val Tyr Tyr Cys 20 25 30 <210> 516 <211> 32 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 516 Gly Thr Pro Ala Arg Phe Ser Gly Ser Ser Leu Gly Gly Lys Ala Ala 1 5 10 15 Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Val Tyr Tyr Cys 20 25 30 <210> 517 <211> 32 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 517 Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Ser Ala Ala 1 5 10 15 Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Val Tyr Tyr Cys 20 25 30 <210> 518 <211> 32 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 518 Gly Thr Pro Ala Arg Phe Ser Gly Ser Ser Leu Gly Gly Ser Ala Ala 1 5 10 15 Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Val Tyr Tyr Cys 20 25 30 <210> 519 <211> 32 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 519 Gly Thr Pro Ala Arg Phe Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala 1 5 10 15 Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys 20 25 30 <210> 520 <211> 32 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 520 Gly Thr Pro Ala Arg Phe Ser Gly Ser Ser Leu Gly Gly Ser Ala Ala 1 5 10 15 Leu Thr Leu Ser Gly Val Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys 20 25 30 <210> 521 <211> 9 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 521 Gly Gly Gly Thr Lys Leu Thr Val Leu 1 5 <210> 522 <211> 25 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 522 Glu Val Gln Leu Leu Glu Ser Gly Gly Gly Ile Val Gln Pro Gly Gly 1 5 10 15 Ser Leu Lys Leu Ser Cys Ala Ala Ser 20 25 <210> 523 <211> 25 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 523 Glu Val Gln Leu Gln Glu Ser Gly Gly Gly Ile Val Gln Pro Gly Gly 1 5 10 15 Ser Leu Lys Leu Ser Cys Ala Ala Ser 20 25 <210> 524 <211> 25 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 524 Glu Val Gln Leu Gln Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 1 5 10 15 Ser Leu Lys Leu Ser Cys Ala Ala Ser 20 25 <210> 525 <211> 25 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 525 Glu Val Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 1 5 10 15 Ser Leu Lys Leu Ser Cys Ala Ala Ser 20 25 <210> 526 <211> 14 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 526 Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala 1 5 10 <210> 527 <211> 32 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 527 Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Val Tyr Leu Gln 1 5 10 15 Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg 20 25 30 <210> 528 <211> 32 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 528 Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln 1 5 10 15 Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg 20 25 30 <210> 529 <211> 11 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 529 Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 1 5 10 <210> 530 <211> 109 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 530 Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly 1 5 10 15 Thr Val Thr Leu Thr Cys Arg Ser Ser Asn Gly Ala Val Thr Ser Ser 20 25 30 Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly 35 40 45 Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr Pro Ala Arg Phe 50 55 60 Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val 65 70 75 80 Gln Pro Glu Asp Glu Ala Val Tyr Tyr Cys Ala Leu Trp Tyr Pro Asn 85 90 95 Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 100 105 <210> 531 <211> 125 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 531 Glu Val Gln Leu Leu Glu Ser Gly Gly Gly Ile Val Gln Pro Gly Gly 1 5 10 15 Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr 20 25 30 Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp 50 55 60 Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr 65 70 75 80 Val Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr 85 90 95 Tyr Cys Val Arg His Glu Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe 100 105 110 Ala His Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 115 120 125 <210> 532 <211> 109 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 532 Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly 1 5 10 15 Thr Val Thr Leu Thr Cys Arg Ser Ser Asn Gly Glu Val Thr Thr Ser 20 25 30 Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly 35 40 45 Leu Ile Gly Gly Thr Ile Lys Arg Ala Pro Gly Thr Pro Ala Arg Phe 50 55 60 Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val 65 70 75 80 Gln Pro Glu Asp Glu Ala Val Tyr Tyr Cys Ala Leu Trp Tyr Pro Asn 85 90 95 Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 100 105 <210> 533 <211> 109 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 533 Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly 1 5 10 15 Thr Val Thr Leu Thr Cys Arg Ser Ser Asn Gly Ala Val Thr Ser Ser 20 25 30 Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly 35 40 45 Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr Pro Ala Arg Phe 50 55 60 Ser Gly Ser Ser Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val 65 70 75 80 Gln Pro Glu Asp Glu Ala Val Tyr Tyr Cys Ala Leu Trp Tyr Pro Asn 85 90 95 Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 100 105 <210> 534 <211> 125 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 534 Glu Val Gln Leu Gln Glu Ser Gly Gly Gly Ile Val Gln Pro Gly Gly 1 5 10 15 Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr 20 25 30 Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp 50 55 60 Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr 65 70 75 80 Val Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr 85 90 95 Tyr Cys Val Arg His Glu Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe 100 105 110 Ala His Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 115 120 125 <210> 535 <211> 109 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 535 Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly 1 5 10 15 Thr Val Thr Leu Thr Cys Arg Ser Ser Asn Gly Ala Val Thr Ser Ser 20 25 30 Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly 35 40 45 Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr Pro Ala Arg Phe 50 55 60 Ser Gly Ser Leu Leu Gly Gly Ser Ala Ala Leu Thr Leu Ser Gly Val 65 70 75 80 Gln Pro Glu Asp Glu Ala Val Tyr Tyr Cys Ala Leu Trp Tyr Pro Asn 85 90 95 Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 100 105 <210> 536 <211> 109 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 536 Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly 1 5 10 15 Thr Val Thr Leu Thr Cys Arg Ser Ser Asn Gly Ala Val Thr Ser Ser 20 25 30 Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly 35 40 45 Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr Pro Ala Arg Phe 50 55 60 Ser Gly Ser Ser Leu Gly Gly Ser Ala Ala Leu Thr Leu Ser Gly Val 65 70 75 80 Gln Pro Glu Asp Glu Ala Val Tyr Tyr Cys Ala Leu Trp Tyr Pro Asn 85 90 95 Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 100 105 <210> 537 <211> 109 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 537 Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly 1 5 10 15 Thr Val Thr Leu Thr Cys Arg Ser Ser Thr Gly Ala Val Thr Thr Ser 20 25 30 Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly 35 40 45 Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr Pro Ala Arg Phe 50 55 60 Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val 65 70 75 80 Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Ala Leu Trp Tyr Ser Asn 85 90 95 Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 100 105 <210> 538 <211> 125 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 538 Glu Val Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 1 5 10 15 Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr 20 25 30 Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp 50 55 60 Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr 65 70 75 80 Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr 85 90 95 Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe 100 105 110 Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 115 120 125 <210> 539 <211> 109 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 539 Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly 1 5 10 15 Thr Val Thr Leu Thr Cys Arg Ser Ser Thr Gly Ala Val Thr Thr Ser 20 25 30 Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly 35 40 45 Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr Pro Ala Arg Phe 50 55 60 Ser Gly Ser Ser Leu Gly Gly Ser Ala Ala Leu Thr Leu Ser Gly Val 65 70 75 80 Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Ala Leu Trp Tyr Ser Asn 85 90 95 Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 100 105 <210> 540 <211> 125 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 540 Glu Val Gln Leu Gln Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 1 5 10 15 Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr 20 25 30 Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ala Arg Ile Arg Ser Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp 50 55 60 Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr 65 70 75 80 Ala Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr 85 90 95 Tyr Cys Val Arg His Gly Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe 100 105 110 Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 115 120 125 <210> 541 <211> 264 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 541 Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly 1 5 10 15 Thr Val Thr Leu Thr Cys Arg Ser Ser Asn Gly Ala Val Thr Ser Ser 20 25 30 Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly 35 40 45 Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr Pro Ala Arg Phe 50 55 60 Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val 65 70 75 80 Gln Pro Glu Asp Glu Ala Val Tyr Tyr Cys Ala Leu Trp Tyr Pro Asn 85 90 95 Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Ala Thr 100 105 110 Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr Gly 115 120 125 Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu Val Gln Leu Leu 130 135 140 Glu Ser Gly Gly Gly Ile Val Gln Pro Gly Gly Ser Leu Lys Leu Ser 145 150 155 160 Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr Ala Met Asn Trp Val 165 170 175 Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser 180 185 190 Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Ser Val Lys Asp Arg 195 200 205 Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Val Tyr Leu Gln Met 210 215 220 Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His 225 230 235 240 Glu Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe Ala His Trp Gly Gln 245 250 255 Gly Thr Leu Val Thr Val Ser Ser 260 <210> 542 <211> 264 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 542 Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly 1 5 10 15 Thr Val Thr Leu Thr Cys Arg Ser Ser Asn Gly Glu Val Thr Thr Ser 20 25 30 Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly 35 40 45 Leu Ile Gly Gly Thr Ile Lys Arg Ala Pro Gly Thr Pro Ala Arg Phe 50 55 60 Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val 65 70 75 80 Gln Pro Glu Asp Glu Ala Val Tyr Tyr Cys Ala Leu Trp Tyr Pro Asn 85 90 95 Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Ala Thr 100 105 110 Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr Gly 115 120 125 Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu Val Gln Leu Leu 130 135 140 Glu Ser Gly Gly Gly Ile Val Gln Pro Gly Gly Ser Leu Lys Leu Ser 145 150 155 160 Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr Ala Met Asn Trp Val 165 170 175 Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser 180 185 190 Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Ser Val Lys Asp Arg 195 200 205 Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Val Tyr Leu Gln Met 210 215 220 Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His 225 230 235 240 Glu Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe Ala His Trp Gly Gln 245 250 255 Gly Thr Leu Val Thr Val Ser Ser 260 <210> 543 <211> 264 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 543 Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly 1 5 10 15 Thr Val Thr Leu Thr Cys Arg Ser Ser Asn Gly Ala Val Thr Ser Ser 20 25 30 Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly 35 40 45 Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr Pro Ala Arg Phe 50 55 60 Ser Gly Ser Ser Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val 65 70 75 80 Gln Pro Glu Asp Glu Ala Val Tyr Tyr Cys Ala Leu Trp Tyr Pro Asn 85 90 95 Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Ala Thr 100 105 110 Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr Gly 115 120 125 Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu Val Gln Leu Gln 130 135 140 Glu Ser Gly Gly Gly Ile Val Gln Pro Gly Gly Ser Leu Lys Leu Ser 145 150 155 160 Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr Ala Met Asn Trp Val 165 170 175 Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser 180 185 190 Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Ser Val Lys Asp Arg 195 200 205 Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Val Tyr Leu Gln Met 210 215 220 Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His 225 230 235 240 Glu Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe Ala His Trp Gly Gln 245 250 255 Gly Thr Leu Val Thr Val Ser Ser 260 <210> 544 <211> 264 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 544 Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly 1 5 10 15 Thr Val Thr Leu Thr Cys Arg Ser Ser Asn Gly Ala Val Thr Ser Ser 20 25 30 Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly 35 40 45 Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr Pro Ala Arg Phe 50 55 60 Ser Gly Ser Leu Leu Gly Gly Ser Ala Ala Leu Thr Leu Ser Gly Val 65 70 75 80 Gln Pro Glu Asp Glu Ala Val Tyr Tyr Cys Ala Leu Trp Tyr Pro Asn 85 90 95 Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Ala Thr 100 105 110 Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr Gly 115 120 125 Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu Val Gln Leu Gln 130 135 140 Glu Ser Gly Gly Gly Ile Val Gln Pro Gly Gly Ser Leu Lys Leu Ser 145 150 155 160 Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr Ala Met Asn Trp Val 165 170 175 Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser 180 185 190 Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Ser Val Lys Asp Arg 195 200 205 Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Val Tyr Leu Gln Met 210 215 220 Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His 225 230 235 240 Glu Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe Ala His Trp Gly Gln 245 250 255 Gly Thr Leu Val Thr Val Ser Ser 260 <210> 545 <211> 264 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 545 Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly 1 5 10 15 Thr Val Thr Leu Thr Cys Arg Ser Ser Asn Gly Ala Val Thr Ser Ser 20 25 30 Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly 35 40 45 Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr Pro Ala Arg Phe 50 55 60 Ser Gly Ser Ser Leu Gly Gly Ser Ala Ala Leu Thr Leu Ser Gly Val 65 70 75 80 Gln Pro Glu Asp Glu Ala Val Tyr Tyr Cys Ala Leu Trp Tyr Pro Asn 85 90 95 Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Ala Thr 100 105 110 Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr Gly 115 120 125 Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu Val Gln Leu Gln 130 135 140 Glu Ser Gly Gly Gly Ile Val Gln Pro Gly Gly Ser Leu Lys Leu Ser 145 150 155 160 Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr Ala Met Asn Trp Val 165 170 175 Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser 180 185 190 Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Ser Val Lys Asp Arg 195 200 205 Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Val Tyr Leu Gln Met 210 215 220 Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His 225 230 235 240 Glu Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe Ala His Trp Gly Gln 245 250 255 Gly Thr Leu Val Thr Val Ser Ser 260 <210> 546 <211> 264 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 546 Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly 1 5 10 15 Thr Val Thr Leu Thr Cys Arg Ser Ser Thr Gly Ala Val Thr Thr Ser 20 25 30 Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly 35 40 45 Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr Pro Ala Arg Phe 50 55 60 Ser Gly Ser Leu Leu Gly Gly Lys Ala Ala Leu Thr Leu Ser Gly Val 65 70 75 80 Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Ala Leu Trp Tyr Ser Asn 85 90 95 Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Ala Thr 100 105 110 Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr Gly 115 120 125 Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu Val Gln Leu Leu 130 135 140 Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser 145 150 155 160 Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr Ala Met Asn Trp Val 165 170 175 Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser 180 185 190 Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Ser Val Lys Asp Arg 195 200 205 Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met 210 215 220 Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His 225 230 235 240 Gly Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe Ala Tyr Trp Gly Gln 245 250 255 Gly Thr Leu Val Thr Val Ser Ser 260 <210> 547 <211> 264 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 547 Glu Leu Val Val Thr Gln Glu Pro Ser Leu Thr Val Ser Pro Gly Gly 1 5 10 15 Thr Val Thr Leu Thr Cys Arg Ser Ser Thr Gly Ala Val Thr Thr Ser 20 25 30 Asn Tyr Ala Asn Trp Val Gln Gln Lys Pro Gly Gln Ala Pro Arg Gly 35 40 45 Leu Ile Gly Gly Thr Asn Lys Arg Ala Pro Gly Thr Pro Ala Arg Phe 50 55 60 Ser Gly Ser Ser Leu Gly Gly Ser Ala Ala Leu Thr Leu Ser Gly Val 65 70 75 80 Gln Pro Glu Asp Glu Ala Glu Tyr Tyr Cys Ala Leu Trp Tyr Ser Asn 85 90 95 Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Ala Thr 100 105 110 Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr Gly 115 120 125 Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu Val Gln Leu Gln 130 135 140 Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Lys Leu Ser 145 150 155 160 Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr Ala Met Asn Trp Val 165 170 175 Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Arg Ile Arg Ser 180 185 190 Lys Tyr Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp Ser Val Lys Asp Arg 195 200 205 Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr Ala Tyr Leu Gln Met 210 215 220 Asn Asn Leu Lys Thr Glu Asp Thr Ala Val Tyr Tyr Cys Val Arg His 225 230 235 240 Gly Asn Phe Gly Asn Ser Tyr Val Ser Trp Phe Ala Tyr Trp Gly Gln 245 250 255 Gly Thr Leu Val Thr Val Ser Ser 260 <210> 548 <211> 256 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 548 Gln Ser Val Leu Thr Gln Pro Pro Ser Ala Ser Gly Thr Pro Gly Gln 1 5 10 15 Arg Val Thr Ile Ser Cys Ser Gly Ser Ser Ser Asn Ile Gly Ser Asn 20 25 30 Tyr Val Tyr Trp Tyr Gln Gln Leu Pro Gly Thr Ala Pro Lys Leu Leu 35 40 45 Ile Tyr Arg Asn Asn Gln Arg Pro Ser Gly Val Pro Asp Arg Phe Ser 50 55 60 Gly Ser Lys Ser Gly Thr Ser Ala Ser Leu Ala Ile Ser Gly Leu Arg 65 70 75 80 Ser Glu Asp Glu Ala Asp Tyr Tyr Cys Ala Ala Trp Asp Asp Ser Leu 85 90 95 Ser Gly Leu Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly 100 105 110 Ala Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr 115 120 125 Thr Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Gln Val Gln 130 135 140 Leu Gln Gln Trp Gly Gly Gly Leu Val Lys Pro Gly Gly Ser Leu Arg 145 150 155 160 Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Ser Tyr Ser Met Asn 165 170 175 Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ser Arg Ile 180 185 190 Asn Ser Asp Gly Ser Ser Thr Asn Tyr Ala Asp Ser Val Lys Gly Arg 195 200 205 Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Leu Tyr Leu Gln Met 210 215 220 Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Arg Glu 225 230 235 240 Leu Arg Trp Gly Asn Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 245 250 255 <210> 549 <211> 255 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 549 Gln Ala Gly Leu Thr Gln Pro Pro Ser Ala Ser Gly Thr Pro Gly Gln 1 5 10 15 Arg Val Thr Leu Ser Cys Ser Gly Ser Tyr Ser Asn Ile Gly Thr Tyr 20 25 30 Tyr Val Tyr Trp Tyr Gln Gln Leu Pro Gly Thr Ala Pro Lys Leu Leu 35 40 45 Ile Tyr Ser Asn Asp Gln Arg Leu Ser Gly Val Pro Asp Arg Phe Ser 50 55 60 Gly Ser Lys Ser Gly Thr Ser Ala Ser Leu Ala Ile Ser Gly Leu Gln 65 70 75 80 Ser Glu Asp Glu Ala Ala Tyr Tyr Cys Ala Ala Trp Asp Asp Ser Leu 85 90 95 Asn Gly Trp Ala Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Ala 100 105 110 Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr 115 120 125 Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Gln Val Gln Leu 130 135 140 Gln Gln Trp Gly Gly Gly Leu Val Lys Pro Gly Gly Ser Leu Arg Leu 145 150 155 160 Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Ser Tyr Ser Met Asn Trp 165 170 175 Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ser Arg Ile Asn 180 185 190 Ser Asp Gly Ser Ser Thr Asn Tyr Ala Asp Ser Val Lys Gly Arg Phe 195 200 205 Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Leu Tyr Leu Gln Met Asn 210 215 220 Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Arg Glu Leu 225 230 235 240 Arg Trp Gly Asn Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 245 250 255 <210> 550 <211> 255 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 550 Gln Pro Gly Leu Thr Gln Pro Pro Ser Ala Ser Gly Thr Pro Gly Gln 1 5 10 15 Arg Val Thr Leu Ser Cys Ser Gly Arg Ser Ser Asn Ile Gly Ser Tyr 20 25 30 Tyr Val Tyr Trp Tyr Gln His Leu Pro Gly Met Ala Pro Lys Leu Leu 35 40 45 Ile Tyr Arg Asn Ser Arg Arg Pro Ser Gly Val Pro Asp Arg Phe Ser 50 55 60 Gly Ser Lys Ser Gly Thr Ser Ala Ser Leu Val Ile Ser Gly Leu Gln 65 70 75 80 Ser Asp Asp Glu Ala Asp Tyr Tyr Cys Ala Ala Trp Asp Asp Ser Leu 85 90 95 Lys Ser Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Ala 100 105 110 Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr 115 120 125 Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Gln Val Gln Leu 130 135 140 Gln Gln Trp Gly Gly Gly Leu Val Lys Pro Gly Gly Ser Leu Arg Leu 145 150 155 160 Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Ser Tyr Ser Met Asn Trp 165 170 175 Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ser Arg Ile Asn 180 185 190 Ser Asp Gly Ser Ser Thr Asn Tyr Ala Asp Ser Val Lys Gly Arg Phe 195 200 205 Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Leu Tyr Leu Gln Met Asn 210 215 220 Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Arg Glu Leu 225 230 235 240 Arg Trp Gly Asn Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 245 250 255 <210> 551 <211> 255 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 551 Gln Ser Val Leu Thr Gln Pro Pro Ser Ala Ser Gly Thr Pro Gly Gln 1 5 10 15 Arg Val Thr Ile Ser Cys Ser Gly Ser Ser Ser Asn Ile Gly Thr Asn 20 25 30 Tyr Val Tyr Trp Tyr Gln Gln Phe Pro Gly Thr Ala Pro Lys Leu Leu 35 40 45 Ile Tyr Ser Asn Asn Gln Arg Pro Ser Gly Val Pro Asp Arg Phe Ser 50 55 60 Gly Ser Lys Ser Gly Thr Ser Gly Ser Leu Ala Ile Ser Gly Leu Gln 65 70 75 80 Ser Glu Asp Glu Ala Asp Tyr Ser Cys Ala Ala Trp Asp Asp Ser Leu 85 90 95 Asn Gly Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Ala 100 105 110 Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr 115 120 125 Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Gln Val Gln Leu 130 135 140 Val Gln Trp Gly Gly Gly Leu Val Lys Pro Gly Gly Ser Leu Arg Leu 145 150 155 160 Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Ser Tyr Ser Met Asn Trp 165 170 175 Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ser Arg Ile Asn 180 185 190 Ser Asp Gly Ser Ser Thr Asn Tyr Ala Asp Ser Val Lys Gly Arg Phe 195 200 205 Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Leu Tyr Leu Gln Met Asn 210 215 220 Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Arg Glu Leu 225 230 235 240 Arg Trp Gly Asn Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 245 250 255 <210> 552 <211> 255 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 552 Gln Pro Gly Leu Thr Gln Pro Pro Ser Ala Ser Gly Thr Pro Gly Gln 1 5 10 15 Arg Val Thr Ile Ser Cys Ser Gly Ser Ser Ser Asn Ile Gly Ser Asn 20 25 30 Tyr Val Tyr Trp Tyr Gln Gln Leu Pro Gly Thr Ala Pro Lys Leu Leu 35 40 45 Ile Tyr Arg Asn Asn Gln Arg Pro Ser Gly Val Pro Asp Arg Leu Ser 50 55 60 Gly Ser Lys Ser Gly Thr Ser Ala Ser Leu Ala Ile Ser Gly Leu Arg 65 70 75 80 Ser Glu Asp Glu Ala Asp Tyr Tyr Cys Ala Ala Trp Asp Asp Ser Leu 85 90 95 Ser Gly Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Ala 100 105 110 Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr 115 120 125 Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Gln Val Gln Leu 130 135 140 Val Gln Trp Gly Gly Gly Leu Val Lys Pro Gly Gly Ser Leu Arg Leu 145 150 155 160 Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Ser Tyr Ser Met Asn Trp 165 170 175 Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ser Arg Ile Asn 180 185 190 Ser Asp Gly Ser Ser Thr Asn Tyr Ala Asp Ser Val Lys Gly Arg Phe 195 200 205 Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Leu Tyr Leu Gln Met Asn 210 215 220 Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Arg Glu Leu 225 230 235 240 Arg Trp Gly Asn Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 245 250 255 <210> 553 <211> 256 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 553 Gln Ala Val Leu Thr Gln Pro Pro Ser Ala Ser Gly Thr Pro Gly Gln 1 5 10 15 Arg Val Thr Ile Ser Cys Ser Gly Ser Ser Ser Asn Ile Gly Ser Tyr 20 25 30 Tyr Val Tyr Trp Tyr Gln Gln Val Pro Gly Ala Ala Pro Lys Leu Leu 35 40 45 Met Arg Leu Asn Asn Gln Arg Pro Ser Gly Val Pro Asp Arg Phe Ser 50 55 60 Gly Ala Lys Ser Gly Thr Ser Ala Ser Leu Val Ile Ser Gly Leu Arg 65 70 75 80 Ser Glu Asp Glu Ala Asp Tyr Tyr Cys Ala Ala Trp Asp Asp Ser Leu 85 90 95 Ser Gly Gln Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly 100 105 110 Ala Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr 115 120 125 Thr Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Gln Val Gln 130 135 140 Leu Gln Gln Trp Gly Gly Gly Leu Val Lys Pro Gly Gly Ser Leu Arg 145 150 155 160 Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Ser Tyr Ser Met Asn 165 170 175 Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ser Arg Ile 180 185 190 Asn Ser Asp Gly Ser Ser Thr Asn Tyr Ala Asp Ser Val Lys Gly Arg 195 200 205 Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Leu Tyr Leu Gln Met 210 215 220 Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Arg Glu 225 230 235 240 Leu Arg Trp Gly Asn Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 245 250 255 <210> 554 <211> 255 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 554 Gln Ala Gly Leu Thr Gln Pro Pro Ser Ala Ser Gly Thr Pro Gly Gln 1 5 10 15 Arg Val Thr Ile Ser Cys Ser Gly Ser Ser Ser Asn Ile Gly Ser Asn 20 25 30 Tyr Val Tyr Trp Tyr Gln Gln Leu Pro Gly Thr Ala Pro Lys Leu Leu 35 40 45 Ile Tyr Arg Asn Asn Gln Arg Pro Ser Gly Val Pro Asp Arg Phe Ser 50 55 60 Gly Ser Lys Ser Gly Thr Ser Ala Ser Leu Ala Ile Ser Gly Leu Arg 65 70 75 80 Ser Glu Asp Glu Ala Asp Tyr Tyr Cys Ala Thr Trp Asp Ala Ser Leu 85 90 95 Ser Gly Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Ala 100 105 110 Thr Pro Pro Glu Thr Gly Ala Glu Thr Glu Ser Pro Gly Glu Thr Thr 115 120 125 Gly Gly Ser Ala Glu Ser Glu Pro Pro Gly Glu Gly Glu Val Gln Leu 130 135 140 Val Gln Trp Gly Gly Gly Leu Val Lys Pro Gly Gly Ser Leu Arg Leu 145 150 155 160 Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Ser Tyr Ser Met Asn Trp 165 170 175 Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ser Arg Ile Asn 180 185 190 Ser Asp Gly Ser Ser Thr Asn Tyr Ala Asp Ser Val Lys Gly Arg Phe 195 200 205 Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Leu Tyr Leu Gln Met Asn 210 215 220 Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Arg Glu Leu 225 230 235 240 Arg Trp Gly Asn Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 245 250 255 <210> 555 <211> 123 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 555 Gln Val Gln Leu Val Gln Ser Gly Ala Glu Val Lys Lys Pro Gly Ala 1 5 10 15 Ser Val Lys Val Ser Cys Lys Ala Ser Gly Phe Asn Ile Lys Asp Thr 20 25 30 Tyr Ile His Trp Val Arg Gln Ala Pro Gly Gln Arg Leu Glu Trp Met 35 40 45 Gly Arg Ile Asp Pro Ala Asn Gly Tyr Thr Lys Tyr Asp Pro Lys Phe 50 55 60 Gln Gly Arg Val Thr Ile Thr Ala Asp Thr Ser Ala Ser Thr Ala Tyr 65 70 75 80 Met Glu Leu Ser Ser Leu Arg Ser Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Glu Gly Tyr Tyr Gly Asn Tyr Gly Val Tyr Ala Met Asp Tyr 100 105 110 Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 115 120 <210> 556 <211> 122 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 556 Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Ser Tyr 20 25 30 Asp Ile His Trp Val Arg Gln Ala Thr Gly Lys Gly Leu Glu Trp Val 35 40 45 Ser Ala Ile Gly Pro Ala Gly Asp Thr Tyr Tyr Pro Gly Ser Val Lys 50 55 60 Gly Arg Phe Thr Ile Ser Arg Glu Asn Ala Lys Asn Ser Leu Tyr Leu 65 70 75 80 Gln Met Asn Ser Leu Arg Ala Gly Asp Thr Ala Val Tyr Tyr Cys Ala 85 90 95 Arg Gly Leu Ile Thr Phe Gly Gly Leu Ile Ala Pro Phe Asp Tyr Trp 100 105 110 Gly Gln Gly Thr Leu Val Thr Val Ser Ser 115 120 <210> 557 <211> 120 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 557 Gln Val Lys Leu Glu Gln Ser Gly Ala Glu Val Val Lys Pro Gly Ala 1 5 10 15 Ser Val Lys Leu Ser Cys Lys Ala Ser Gly Phe Asn Ile Lys Asp Ser 20 25 30 Tyr Met His Trp Leu Arg Gln Gly Pro Gly Gln Arg Leu Glu Trp Ile 35 40 45 Gly Trp Ile Asp Pro Glu Asn Gly Asp Thr Glu Tyr Ala Pro Lys Phe 50 55 60 Gln Gly Lys Ala Thr Phe Thr Thr Asp Thr Ser Ala Asn Thr Ala Tyr 65 70 75 80 Leu Gly Leu Ser Ser Leu Arg Pro Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Asn Glu Gly Thr Pro Thr Gly Pro Tyr Tyr Phe Asp Tyr Trp Gly Gln 100 105 110 Gly Thr Leu Val Thr Val Ser Ser 115 120 <210> 558 <211> 121 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 558 Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Asn Ile Lys Asp Thr 20 25 30 Tyr Met His Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ala Arg Ile Asp Pro Ala Asn Gly Asn Ser Lys Tyr Ala Asp Ser Val 50 55 60 Lys Gly Arg Phe Thr Ile Ser Ala Asp Thr Ser Lys Asn Thr Ala Tyr 65 70 75 80 Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Pro Phe Gly Tyr Tyr Val Ser Asp Tyr Ala Met Ala Tyr Trp Gly 100 105 110 Gln Gly Thr Leu Val Thr Val Ser Ser 115 120 <210> 559 <211> 121 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 559 Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Asn Ile Lys Asp Thr 20 25 30 Tyr Met His Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ala Arg Ile Asp Pro Ala Asn Gly Asn Ser Lys Tyr Val Pro Lys Phe 50 55 60 Gln Gly Arg Ala Thr Ile Ser Ala Asp Thr Ser Lys Asn Thr Ala Tyr 65 70 75 80 Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Pro Phe Gly Tyr Tyr Val Ser Asp Tyr Ala Met Ala Tyr Trp Gly 100 105 110 Gln Gly Thr Leu Val Thr Val Ser Ser 115 120 <210> 560 <211> 119 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 560 Glu Val Gln Leu Val Glu Ser Gly Gly Gly Val Val Gln Pro Gly Arg 1 5 10 15 Ser Leu Arg Leu Ser Cys Ser Ala Ser Gly Phe Asp Phe Thr Thr Tyr 20 25 30 Trp Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile 35 40 45 Gly Glu Ile His Pro Asp Ser Ser Thr Ile Asn Tyr Ala Pro Ser Leu 50 55 60 Lys Asp Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Leu Phe 65 70 75 80 Leu Gln Met Asp Ser Leu Arg Pro Glu Asp Thr Gly Val Tyr Phe Cys 85 90 95 Ala Ser Leu Tyr Phe Gly Phe Pro Trp Phe Ala Tyr Trp Gly Gln Gly 100 105 110 Thr Pro Val Thr Val Ser Ser 115 <210> 561 <211> 121 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 561 Glu Val Lys Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Thr Ser Gly Phe Thr Phe Thr Asp Tyr 20 25 30 Tyr Met Asn Trp Val Arg Gln Pro Pro Gly Lys Ala Leu Glu Trp Leu 35 40 45 Gly Phe Ile Gly Asn Lys Ala Asn Gly Tyr Thr Thr Glu Tyr Ser Ala 50 55 60 Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Lys Ser Gln Ser Ile 65 70 75 80 Leu Tyr Leu Gln Met Asn Thr Leu Arg Ala Glu Asp Ser Ala Thr Tyr 85 90 95 Tyr Cys Thr Arg Asp Arg Gly Leu Arg Phe Tyr Phe Asp Tyr Trp Gly 100 105 110 Gln Gly Thr Thr Leu Thr Val Ser Ser 115 120 <210> 562 <211> 121 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 562 Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Arg 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Val Ser Ser Tyr 20 25 30 Trp Met His Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Gly Phe Ile Arg Asn Lys Ala Asn Gly Gly Thr Thr Glu Tyr Ala Ala 50 55 60 Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asp Ser Lys Asn Thr 65 70 75 80 Leu Tyr Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr 85 90 95 Tyr Cys Ala Arg Asp Arg Gly Leu Arg Phe Tyr Phe Asp Tyr Trp Gly 100 105 110 Gln Gly Thr Thr Val Thr Val Ser Ser 115 120 <210> 563 <211> 124 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 563 Gln Val Gln Leu Gln Gln Ser Gly Ala Glu Leu Val Arg Pro Gly Ser 1 5 10 15 Ser Val Lys Ile Ser Cys Lys Ala Ser Gly Tyr Ala Phe Ser Ser Tyr 20 25 30 Trp Met Asn Trp Val Lys Gln Arg Pro Gly Gln Gly Leu Glu Trp Ile 35 40 45 Gly Gln Ile Trp Pro Gly Asp Gly Asp Thr Asn Tyr Asn Gly Lys Phe 50 55 60 Lys Gly Lys Ala Thr Leu Thr Ala Asp Glu Ser Ser Ser Thr Ala Tyr 65 70 75 80 Met Gln Leu Ser Ser Leu Ala Ser Glu Asp Ser Ala Val Tyr Phe Cys 85 90 95 Ala Arg Arg Glu Thr Thr Thr Val Gly Arg Tyr Tyr Tyr Ala Met Asp 100 105 110 Tyr Trp Gly Gln Gly Thr Thr Val Thr Val Ser Ser 115 120 <210> 564 <211> 122 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 564 Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Arg 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Asp Tyr 20 25 30 Ala Met His Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ser Thr Ile Ser Trp Asn Ser Gly Ser Ile Gly Tyr Ala Asp Ser Val 50 55 60 Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Lys Ser Leu Tyr 65 70 75 80 Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Leu Tyr Tyr Cys 85 90 95 Ala Lys Asp Ile Gln Tyr Gly Asn Tyr Tyr Tyr Gly Met Asp Val Trp 100 105 110 Gly Gln Gly Thr Thr Val Thr Val Ser Ser 115 120 <210> 565 <211> 122 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 565 Gln Ala Tyr Leu Gln Gln Ser Gly Ala Glu Leu Val Arg Pro Gly Ala 1 5 10 15 Ser Val Lys Met Ser Cys Lys Ala Ser Gly Tyr Thr Phe Thr Ser Tyr 20 25 30 Asn Met His Trp Val Lys Gln Thr Pro Arg Gln Gly Leu Glu Trp Ile 35 40 45 Gly Ala Ile Tyr Pro Gly Asn Gly Asp Thr Ser Tyr Asn Gln Lys Phe 50 55 60 Lys Gly Lys Ala Thr Leu Thr Val Asp Lys Ser Ser Ser Thr Ala Tyr 65 70 75 80 Met Gln Leu Ser Ser Leu Thr Ser Glu Asp Ser Ala Val Tyr Phe Cys 85 90 95 Ala Arg Val Val Tyr Tyr Ser Asn Ser Tyr Trp Tyr Phe Asp Val Trp 100 105 110 Gly Thr Gly Thr Thr Val Thr Val Ser Gly 115 120 <210> 566 <211> 119 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 566 Gln Val Gln Leu Val Gln Ser Gly Ala Glu Val Lys Lys Pro Gly Ser 1 5 10 15 Ser Val Lys Val Ser Cys Lys Ala Ser Gly Tyr Ala Phe Ser Tyr Ser 20 25 30 Trp Ile Asn Trp Val Arg Gln Ala Pro Gly Gln Gly Leu Glu Trp Met 35 40 45 Gly Arg Ile Phe Pro Gly Asp Gly Asp Thr Asp Tyr Asn Gly Lys Phe 50 55 60 Lys Gly Arg Val Thr Ile Thr Ala Asp Lys Ser Thr Ser Thr Ala Tyr 65 70 75 80 Met Glu Leu Ser Ser Leu Arg Ser Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Asn Val Phe Asp Gly Tyr Trp Leu Val Tyr Trp Gly Gln Gly 100 105 110 Thr Leu Val Thr Val Ser Ser 115 <210> 567 <211> 122 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 567 Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Tyr Thr Phe Thr Ser Tyr 20 25 30 Asn Met His Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Gly Ala Ile Tyr Pro Gly Asn Gly Asp Thr Ser Tyr Asn Gln Lys Phe 50 55 60 Lys Gly Arg Phe Thr Ile Ser Val Asp Lys Ser Lys Asn Thr Leu Tyr 65 70 75 80 Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Val Val Tyr Tyr Ser Asn Ser Tyr Trp Tyr Phe Asp Val Trp 100 105 110 Gly Gln Gly Thr Leu Val Thr Val Ser Ser 115 120 <210> 568 <211> 121 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 568 Gln Val Gln Leu Gln Gln Pro Gly Ala Glu Leu Val Lys Pro Gly Ala 1 5 10 15 Ser Val Lys Met Ser Cys Lys Ala Ser Gly Tyr Thr Phe Thr Ser Tyr 20 25 30 Asn Met His Trp Val Lys Gln Thr Pro Gly Arg Gly Leu Glu Trp Ile 35 40 45 Gly Ala Ile Tyr Pro Gly Asn Gly Asp Thr Ser Tyr Asn Gln Lys Phe 50 55 60 Lys Gly Lys Ala Thr Leu Thr Ala Asp Lys Ser Ser Ser Thr Ala Tyr 65 70 75 80 Met Gln Leu Ser Ser Leu Thr Ser Glu Asp Ser Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Ser Thr Tyr Tyr Gly Gly Asp Trp Tyr Phe Asn Val Trp Gly 100 105 110 Ala Gly Thr Thr Val Thr Val Ser Ala 115 120 <210> 569 <211> 122 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 569 Gln Ala Tyr Leu Gln Gln Ser Gly Ala Glu Leu Val Arg Pro Gly Ala 1 5 10 15 Ser Val Lys Met Ser Cys Lys Ala Ser Gly Tyr Thr Phe Thr Ser Tyr 20 25 30 Asn Met His Trp Val Lys Gln Thr Pro Arg Gln Gly Leu Glu Trp Ile 35 40 45 Gly Ala Ile Tyr Pro Gly Asn Gly Asp Thr Ser Tyr Asn Gln Lys Phe 50 55 60 Lys Gly Lys Ala Thr Leu Thr Val Asp Lys Ser Ser Ser Thr Ala Tyr 65 70 75 80 Met Gln Leu Ser Ser Leu Thr Ser Glu Asp Ser Ala Val Tyr Phe Cys 85 90 95 Ala Arg Val Val Tyr Tyr Ser Asn Ser Tyr Trp Tyr Phe Asp Val Trp 100 105 110 Gly Thr Gly Thr Thr Thr Val Thr Val Ser Ala 115 120 <210> 570 <211> 114 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 570 Gln Leu Val Gln Ser Gly Ala Glu Val Lys Lys Pro Gly Ser Ser Val 1 5 10 15 Lys Val Ser Cys Lys Ala Ser Gly Tyr Thr Ile Thr Asp Ser Asn Ile 20 25 30 His Trp Val Arg Gln Ala Pro Gly Gln Ser Leu Glu Trp Ile Gly Tyr 35 40 45 Ile Tyr Pro Tyr Asn Gly Gly Thr Asp Tyr Asn Gln Lys Phe Lys Asn 50 55 60 Arg Ala Thr Leu Thr Val Asp Asn Pro Thr Asn Thr Ala Tyr Met Glu 65 70 75 80 Leu Ser Ser Leu Arg Ser Glu Asp Thr Asp Phe Tyr Tyr Cys Val Asn 85 90 95 Gly Asn Pro Trp Leu Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr Val 100 105 110 Ser Ser <210> 571 <211> 122 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 571 Glu Val Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Val Ser Gly Phe Thr Phe Asn Ser Phe 20 25 30 Ala Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ser Ala Ile Ser Gly Ser Gly Gly Gly Thr Tyr Tyr Ala Asp Ser Val 50 55 60 Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 65 70 75 80 Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Phe Cys 85 90 95 Ala Lys Asp Lys Ile Leu Trp Phe Gly Glu Pro Val Phe Asp Tyr Trp 100 105 110 Gly Gln Gly Thr Leu Val Thr Val Ser Ser 115 120 <210> 572 <211> 118 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 572 Gln Ile Gln Leu Val Gln Ser Gly Pro Glu Val Lys Lys Pro Gly Glu 1 5 10 15 Thr Val Lys Ile Ser Cys Lys Ala Ser Gly Tyr Thr Phe Thr Asn Tyr 20 25 30 Gly Met Asn Trp Val Lys Gln Ala Pro Gly Lys Gly Leu Lys Trp Met 35 40 45 Gly Trp Ile Asn Thr Tyr Thr Gly Glu Pro Thr Tyr Ala Asp Ala Phe 50 55 60 Lys Gly Arg Phe Ala Phe Ser Leu Glu Thr Ser Ala Ser Thr Ala Tyr 65 70 75 80 Leu Gln Ile Asn Asn Leu Lys Asn Glu Asp Thr Ala Thr Tyr Phe Cys 85 90 95 Ala Arg Asp Tyr Gly Asp Tyr Gly Met Asp Tyr Trp Gly Gln Gly Thr 100 105 110 Ser Val Thr Val Ser Ser 115 <210> 573 <211> 118 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 573 Gln Val Gln Leu Gln Gln Ser Gly Thr Glu Leu Met Thr Pro Gly Ala 1 5 10 15 Ser Val Thr Met Ser Cys Lys Thr Ser Gly Tyr Thr Phe Ser Thr Tyr 20 25 30 Trp Ile Glu Trp Val Lys Gln Arg Pro Gly His Gly Leu Glu Trp Ile 35 40 45 Gly Glu Ile Leu Gly Pro Ser Gly Tyr Thr Asp Tyr Asn Glu Lys Phe 50 55 60 Lys Ala Lys Ala Thr Phe Thr Ala Asp Thr Ser Ser Asn Thr Ala Tyr 65 70 75 80 Met Gln Leu Ser Ser Leu Ala Ser Glu Asp Ser Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Trp Asp Arg Leu Tyr Ala Met Asp Tyr Trp Gly Gly Gly Thr 100 105 110 Ser Val Thr Val Ser Ser 115 <210> 574 <211> 118 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 574 Gln Val Gln Leu Val Glu Ser Gly Gly Gly Val Val Gln Pro Gly Arg 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Ser Tyr 20 25 30 Ile Met His Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ala Val Ile Ser Tyr Asp Gly Arg Asn Lys Tyr Tyr Ala Asp Ser Val 50 55 60 Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 65 70 75 80 Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Asp Thr Asp Gly Tyr Asp Phe Asp Tyr Trp Gly Gln Gly Thr 100 105 110 Leu Val Thr Val Ser Ser 115 <210> 575 <211> 119 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 575 Gln Ile Gln Leu Val Glu Ser Gly Gly Gly Val Val Gln Pro Gly Arg 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Gly Tyr Tyr 20 25 30 Ala Met His Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ala Val Ile Ser Tyr Asp Gly Ser Ile Lys Tyr Tyr Ala Asp Ser Val 50 55 60 Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 65 70 75 80 Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Glu Gly Pro Tyr Ser Asn Tyr Leu Asp Tyr Trp Gly Gln Gly 100 105 110 Thr Leu Val Thr Val Ser Ser 115 <210> 576 <211> 118 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 576 Gln Val Gln Leu Val Glu Ser Gly Gly Gly Val Val Gln Pro Gly Arg 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Thr Ser Gly Phe Thr Phe Ser Asp Tyr 20 25 30 Gly Met His Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ala Val Ile Trp Tyr Asp Gly Ser Asn Lys Tyr Tyr Ala Asp Ser Val 50 55 60 Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Lys Thr Leu Ser 65 70 75 80 Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Asp Ser Ile Met Val Arg Gly Asp Tyr Trp Gly Gln Gly Thr 100 105 110 Leu Val Thr Val Ser Ser 115 <210> 577 <211> 118 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 577 Gln Val Gln Leu Val Glu Ser Gly Gly Gly Val Val Gln Pro Gly Arg 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Asp His 20 25 30 Gly Met His Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ala Val Ile Trp Tyr Asp Gly Ser Asn Lys Tyr Tyr Ala Asp Ser Val 50 55 60 Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 65 70 75 80 Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Asp Ser Ile Met Val Arg Gly Asp Tyr Trp Gly Gln Gly Thr 100 105 110 Leu Val Thr Val Ser Ser 115 <210> 578 <211> 122 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 578 Gln Val Gln Leu Gln Glu Ser Gly Pro Gly Leu Val Lys Pro Ser Glu 1 5 10 15 Thr Leu Ser Leu Thr Cys Thr Val Ser Gly Gly Ser Val Ser Ser Asp 20 25 30 Tyr Tyr Tyr Trp Ser Trp Ile Arg Gln Pro Pro Gly Lys Gly Leu Glu 35 40 45 Trp Leu Gly Tyr Ile Tyr Tyr Ser Gly Ser Thr Asn Tyr Asn Pro Ser 50 55 60 Leu Lys Ser Arg Val Thr Ile Ser Val Asp Thr Ser Lys Asn Gln Phe 65 70 75 80 Ser Leu Lys Leu Arg Ser Val Thr Thr Ala Asp Thr Ala Val Tyr Tyr 85 90 95 Cys Ala Arg Gly Asp Gly Asp Tyr Gly Gly Asn Cys Phe Asp Tyr Trp 100 105 110 Gly Gln Gly Thr Leu Val Thr Val Ser Ser 115 120 <210> 579 <211> 117 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 579 Gln Val Gln Leu Val Gln Ser Gly Ala Glu Val Lys Lys Pro Gly Ala 1 5 10 15 Ser Val Lys Val Ser Cys Lys Ala Ser Gly Tyr Thr Phe Thr Ser Tyr 20 25 30 Gly Phe Ser Trp Val Arg Gln Ala Pro Gly Gln Gly Leu Glu Trp Met 35 40 45 Gly Trp Ile Ser Ala Ser Asn Gly Asn Thr Tyr Tyr Ala Gln Lys Leu 50 55 60 Gln Gly Arg Val Thr Met Thr Thr Asp Thr Ser Thr Ser Thr Ala Tyr 65 70 75 80 Met Glu Leu Arg Ser Leu Arg Ser Asp Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Val Tyr Ala Asp Tyr Ala Asp Tyr Trp Gly Gln Gly Thr Leu 100 105 110 Val Thr Val Ser Ser 115 <210> 580 <211> 115 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 580 Gln Val Gln Leu Val Gln Ser Gly Ala Glu Val Lys Lys Pro Gly Ala 1 5 10 15 Ser Val Lys Val Ser Cys Lys Ala Ser Gly Tyr Thr Phe Thr Asp Tyr 20 25 30 Tyr Met His Trp Val Arg Gln Ala Pro Gly Gln Gly Leu Glu Trp Met 35 40 45 Gly Arg Val Asn Pro Asn Arg Arg Gly Thr Thr Tyr Asn Gln Lys Phe 50 55 60 Glu Gly Arg Val Thr Met Thr Thr Asp Thr Ser Thr Ser Thr Ala Tyr 65 70 75 80 Met Glu Leu Arg Ser Leu Arg Ser Asp Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Ala Asn Trp Leu Asp Tyr Trp Gly Gln Gly Thr Thr Val Thr 100 105 110 Val Ser Ser 115 <210> 581 <211> 119 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 581 Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Tyr Thr Phe Thr Ser Tyr 20 25 30 Trp Leu His Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Gly Met Ile Asp Pro Ser Asn Ser Asp Thr Arg Phe Asn Pro Asn Phe 50 55 60 Lys Asp Arg Phe Thr Ile Ser Ala Asp Thr Ser Lys Asn Thr Ala Tyr 65 70 75 80 Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Thr Tyr Arg Ser Tyr Val Thr Pro Leu Asp Tyr Trp Gly Gln Gly 100 105 110 Thr Leu Val Thr Val Ser Ser 115 <210> 582 <211> 125 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 582 Gln Val Gln Leu Val Glu Ser Gly Gly Gly Val Val Gln Pro Gly Arg 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Ser Tyr 20 25 30 Gly Met His Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ala Val Ile Trp Tyr Asp Gly Ser Asn Lys Tyr Tyr Ala Asp Ser Val 50 55 60 Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 65 70 75 80 Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Asp Pro Arg Gly Ala Thr Leu Tyr Tyr Tyr Tyr Tyr Gly Met 100 105 110 Asp Val Trp Gly Gln Gly Thr Thr Val Thr Val Ser Ser 115 120 125 <210> 583 <211> 118 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 583 Gln Val Gln Leu Val Glu Ser Gly Gly Gly Val Val Gln Pro Gly Arg 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Ser Tyr 20 25 30 Thr Met His Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Thr Phe Ile Ser Tyr Asp Gly Asn Asn Lys Tyr Tyr Ala Asp Ser Val 50 55 60 Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 65 70 75 80 Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Ile Tyr Tyr Cys 85 90 95 Ala Arg Thr Gly Trp Leu Gly Pro Phe Asp Tyr Trp Gly Gln Gly Thr 100 105 110 Leu Val Thr Val Ser Ser 115 <210> 584 <211> 123 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 584 Gln Val Gln Leu Gln Glu Ser Gly Pro Gly Leu Val Lys Pro Ser Gln 1 5 10 15 Thr Leu Ser Leu Thr Cys Thr Val Ser Gly Gly Ser Ile Ser Ser Gly 20 25 30 Gly Tyr Tyr Trp Ser Trp Ile Arg Gln His Pro Gly Lys Gly Leu Glu 35 40 45 Trp Ile Gly Ile Ile Tyr Tyr Ser Gly Ser Thr Tyr Tyr Asn Pro Ser 50 55 60 Leu Lys Ser Arg Val Thr Ile Ser Val Asp Thr Ser Lys Asn Gln Phe 65 70 75 80 Ser Leu Lys Leu Asn Ser Val Thr Ala Ala Asp Thr Ala Val Phe Tyr 85 90 95 Cys Ala Arg Val Ala Ile Val Thr Thr Ile Pro Gly Gly Met Asp Val 100 105 110 Trp Gly Gln Gly Thr Thr Val Thr Val Ser Ser 115 120 <210> 585 <211> 120 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 585 Glu Val Gln Leu Leu Glu Gln Ser Gly Ala Glu Leu Val Arg Pro Gly 1 5 10 15 Thr Ser Val Lys Ile Ser Cys Lys Ala Ser Gly Tyr Ala Phe Thr Asn 20 25 30 Tyr Trp Leu Gly Trp Val Lys Gln Arg Pro Gly His Gly Leu Glu Trp 35 40 45 Ile Gly Asp Ile Phe Pro Gly Ser Gly Asn Ile His Tyr Asn Glu Lys 50 55 60 Phe Lys Gly Lys Ala Thr Leu Thr Ala Asp Lys Ser Ser Ser Thr Ala 65 70 75 80 Tyr Met Gln Leu Ser Ser Leu Thr Phe Glu Asp Ser Ala Val Tyr Phe 85 90 95 Cys Ala Arg Leu Arg Asn Trp Asp Glu Pro Met Asp Tyr Trp Gly Gln 100 105 110 Gly Thr Thr Val Thr Val Ser Ser 115 120 <210> 586 <211> 127 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 586 Glu Val Gln Leu Leu Glu Ser Gly Gly Gly Val Val Gln Pro Gly Arg 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Ser Tyr 20 25 30 Gly Met His Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ala Val Ile Ser Tyr Asp Gly Ser Asn Lys Tyr Tyr Ala Asp Ser Val 50 55 60 Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 65 70 75 80 Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Lys Asp Met Gly Trp Gly Ser Gly Trp Arg Pro Tyr Tyr Tyr Tyr 100 105 110 Gly Met Asp Val Trp Gly Gln Gly Thr Thr Val Thr Val Ser Ser 115 120 125 <210> 587 <211> 116 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 587 Gln Val Gln Leu Gln Gln Ser Gly Ala Glu Leu Val Arg Pro Gly Thr 1 5 10 15 Ser Val Lys Val Ser Cys Lys Ala Ser Gly Tyr Ala Phe Thr Asn Tyr 20 25 30 Leu Ile Glu Trp Val Lys Gln Arg Pro Gly Gln Gly Leu Glu Trp Ile 35 40 45 Gly Val Ile Asn Pro Gly Ser Gly Gly Thr Asn Tyr Asn Glu Lys Phe 50 55 60 Lys Gly Lys Ala Thr Leu Thr Ala Asp Lys Ser Ser Ser Thr Ala Tyr 65 70 75 80 Met Gln Leu Ser Ser Leu Thr Ser Asp Asp Ser Ala Val Tyr Phe Cys 85 90 95 Ala Arg Asp Gly Pro Trp Phe Ala Tyr Trp Gly Gln Gly Thr Leu Val 100 105 110 Thr Val Ser Ala 115 <210> 588 <211> 116 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 588 Gln Ile Gln Leu Val Gln Ser Gly Pro Glu Leu Lys Lys Pro Gly Glu 1 5 10 15 Thr Val Lys Ile Ser Cys Lys Ala Ser Gly Tyr Thr Phe Thr Asn Tyr 20 25 30 Gly Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Lys Trp Met 35 40 45 Gly Trp Ile Asn Thr Tyr Thr Gly Glu Pro Thr Tyr Ala Asp Asp Phe 50 55 60 Lys Gly Arg Phe Val Phe Ser Leu Glu Thr Ser Ala Ser Thr Ala Phe 65 70 75 80 Leu Gln Leu Asn Asn Leu Arg Ser Glu Asp Thr Ala Thr Tyr Phe Cys 85 90 95 Val Arg Phe Ile Ser Lys Gly Asp Tyr Trp Gly Gln Gly Thr Ser Val 100 105 110 Thr Val Ser Ser 115 <210> 589 <211> 114 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 589 Val Gln Leu Gln Gln Ser Asp Ala Glu Leu Val Lys Pro Gly Ala Ser 1 5 10 15 Val Lys Ile Ser Cys Lys Ala Ser Gly Tyr Thr Phe Thr Asp His Ala 20 25 30 Ile His Trp Val Lys Gln Asn Pro Glu Gln Gly Leu Glu Trp Ile Gly 35 40 45 Tyr Phe Ser Pro Gly Asn Asp Asp Phe Lys Tyr Asn Glu Arg Phe Lys 50 55 60 Gly Lys Ala Thr Leu Thr Ala Asp Lys Ser Ser Ser Thr Ala Tyr Val 65 70 75 80 Gln Leu Asn Ser Leu Thr Ser Glu Asp Ser Ala Val Tyr Phe Cys Thr 85 90 95 Arg Ser Leu Asn Met Ala Tyr Trp Gly Gln Gly Thr Ser Val Thr Val 100 105 110 Ser Ser <210> 590 <211> 116 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 590 Glu Val Gln Leu Val Gln Ser Gly Pro Glu Val Lys Lys Pro Gly Ala 1 5 10 15 Ser Val Lys Val Ser Cys Lys Ala Ser Gly Tyr Thr Phe Thr Asn Tyr 20 25 30 Gly Met Asn Trp Val Arg Gln Ala Pro Gly Gln Gly Leu Glu Trp Met 35 40 45 Gly Trp Ile Asn Thr Tyr Thr Gly Glu Pro Thr Tyr Gly Glu Asp Phe 50 55 60 Lys Gly Arg Phe Ala Phe Ser Leu Asp Thr Ser Ala Ser Thr Ala Tyr 65 70 75 80 Met Glu Leu Ser Ser Leu Arg Ser Glu Asp Thr Ala Val Tyr Phe Cys 85 90 95 Ala Arg Phe Gly Asn Tyr Val Asp Tyr Trp Gly Gln Gly Ser Leu Val 100 105 110 Thr Val Ser Ser 115 <210> 591 <211> 116 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 591 Glu Val Gln Leu Val Gln Ser Gly Pro Gly Leu Val Gln Pro Gly Gly 1 5 10 15 Ser Val Arg Ile Ser Cys Ala Ala Ser Gly Tyr Thr Phe Thr Asn Tyr 20 25 30 Gly Met Asn Trp Val Lys Gln Ala Pro Gly Lys Gly Leu Glu Trp Met 35 40 45 Gly Trp Ile Asn Thr Tyr Thr Gly Glu Ser Thr Tyr Ala Asp Ser Phe 50 55 60 Lys Gly Arg Phe Thr Phe Ser Leu Asp Thr Ser Ala Ser Ala Ala Tyr 65 70 75 80 Leu Gln Ile Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Phe Ala Ile Lys Gly Asp Tyr Trp Gly Gln Gly Thr Leu Leu 100 105 110 Thr Val Ser Ser 115 <210> 592 <211> 116 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 592 Glu Val Gln Leu Val Gln Ser Gly Pro Gly Leu Val Gln Pro Gly Gly 1 5 10 15 Ser Val Arg Ile Ser Cys Ala Ala Ser Gly Tyr Thr Phe Thr Asn Tyr 20 25 30 Gly Met Asn Trp Val Lys Gln Ala Pro Gly Lys Gly Leu Glu Trp Met 35 40 45 Gly Trp Ile Asn Thr Tyr Thr Gly Glu Ser Thr Tyr Ala Asp Ser Phe 50 55 60 Lys Gly Arg Phe Thr Phe Ser Leu Asp Thr Ser Ala Ser Ala Ala Tyr 65 70 75 80 Leu Gln Ile Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Phe Ala Ile Lys Gly Asp Tyr Trp Gly Gln Gly Thr Leu Leu 100 105 110 Thr Val Ser Ser 115 <210> 593 <211> 128 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 593 Glu Val Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser His Tyr 20 25 30 Met Met Ala Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ser Arg Ile Gly Pro Ser Gly Gly Pro Thr His Tyr Ala Asp Ser Val 50 55 60 Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 65 70 75 80 Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Gly Tyr Asp Ser Gly Tyr Asp Tyr Val Ala Val Ala Gly Pro Ala 100 105 110 Glu Tyr Phe Gln His Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 115 120 125 <210> 594 <211> 119 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 594 Glu Val Gln Leu Val Glu Ser Gly Gly Gly Val Val Gln Pro Gly Arg 1 5 10 15 Ser Leu Arg Leu Ser Cys Ser Ala Ser Gly Phe Thr Phe Ser Gly Tyr 20 25 30 Gly Leu Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ala Met Ile Ser Ser Gly Gly Ser Tyr Thr Tyr Tyr Ala Asp Ser Val 50 55 60 Lys Gly Arg Phe Ala Ile Ser Arg Asp Asn Ala Lys Asn Thr Leu Phe 65 70 75 80 Leu Gln Met Asp Ser Leu Arg Pro Glu Asp Thr Gly Val Tyr Phe Cys 85 90 95 Ala Arg His Gly Asp Asp Pro Ala Trp Phe Ala Tyr Trp Gly Gln Gly 100 105 110 Thr Pro Val Thr Val Ser Ser 115 <210> 595 <211> 118 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 595 Gln Val Gln Leu Val Gln Ser Gly Ala Glu Val Val Lys Pro Gly Ala 1 5 10 15 Ser Val Lys Ile Ser Cys Lys Ala Ser Gly Tyr Thr Phe Thr Gly Tyr 20 25 30 Phe Met Asn Trp Val Lys Gln Ser Pro Gly Gln Ser Leu Glu Trp Ile 35 40 45 Gly Arg Ile His Pro Tyr Asp Gly Asp Thr Phe Tyr Asn Gln Lys Phe 50 55 60 Gln Gly Lys Ala Thr Leu Thr Val Asp Lys Ser Ser Asn Thr Ala His 65 70 75 80 Met Glu Leu Leu Ser Leu Thr Ser Glu Asp Phe Ala Val Tyr Tyr Cys 85 90 95 Thr Arg Tyr Asp Gly Ser Arg Ala Met Asp Tyr Trp Gly Gln Gly Thr 100 105 110 Thr Val Thr Val Ser Ser 115 <210> 596 <211> 118 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 596 Gln Val Gln Leu Val Gln Ser Gly Ala Glu Val Val Lys Pro Gly Ala 1 5 10 15 Ser Val Lys Ile Ser Cys Lys Ala Ser Gly Tyr Thr Phe Thr Gly Tyr 20 25 30 Phe Met Asn Trp Val Lys Gln Ser Pro Gly Gln Ser Leu Glu Trp Ile 35 40 45 Gly Arg Ile His Pro Tyr Asp Gly Asp Thr Phe Tyr Asn Gln Lys Phe 50 55 60 Gln Gly Lys Ala Thr Leu Thr Val Asp Lys Ser Ser Asn Thr Ala His 65 70 75 80 Met Glu Leu Leu Ser Leu Thr Ser Glu Asp Phe Ala Val Tyr Tyr Cys 85 90 95 Thr Arg Tyr Asp Gly Ser Arg Ala Met Asp Tyr Trp Gly Gln Gly Thr 100 105 110 Thr Val Thr Val Ser Ser 115 <210> 597 <211> 109 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 597 Gly Pro Glu Leu Val Lys Pro Gly Ala Ser Val Lys Ile Ser Cys Lys 1 5 10 15 Ala Ser Asp Tyr Ser Phe Thr Gly Tyr Phe Met Asn Trp Val Met Gln 20 25 30 Ser His Gly Lys Ser Leu Glu Trp Ile Gly Arg Ile Phe Pro Tyr Asn 35 40 45 Gly Asp Thr Phe Tyr Asn Gln Lys Phe Lys Gly Arg Ala Thr Leu Thr 50 55 60 Val Asp Lys Ser Ser Ser Thr Ala His Met Glu Leu Arg Ser Leu Ala 65 70 75 80 Ser Glu Asp Ser Ala Val Tyr Phe Cys Ala Arg Gly Thr His Tyr Phe 85 90 95 Asp Tyr Trp Gly Gln Gly Thr Thr Leu Thr Val Ser Ser 100 105 <210> 598 <211> 115 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 598 Gln Val Gln Leu Val Gln Ser Gly Ala Glu Val Lys Lys Pro Gly Ala 1 5 10 15 Ser Val Lys Val Ser Cys Lys Ala Ser Gly Tyr Thr Phe Thr Asp Tyr 20 25 30 Glu Met His Trp Val Arg Gln Ala Pro Gly Gln Gly Leu Glu Trp Met 35 40 45 Gly Ala Leu Asp Pro Lys Thr Gly Asp Thr Ala Tyr Ser Gln Lys Phe 50 55 60 Lys Gly Arg Val Thr Leu Thr Ala Asp Lys Ser Thr Ser Thr Ala Tyr 65 70 75 80 Met Glu Leu Ser Ser Leu Thr Ser Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Thr Arg Phe Tyr Ser Tyr Thr Tyr Trp Gly Gln Gly Thr Leu Val Thr 100 105 110 Val Ser Ser 115 <210> 599 <211> 117 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 599 Glu Val Gln Leu Val Gln Ser Gly Ala Glu Val Lys Lys Pro Gly Glu 1 5 10 15 Ser Leu Lys Ile Ser Cys Lys Gly Ser Gly Tyr Ser Phe Thr Ser Tyr 20 25 30 Trp Ile Ala Trp Val Arg Gln Met Pro Gly Lys Gly Leu Glu Trp Met 35 40 45 Gly Ile Ile Phe Pro Gly Asp Ser Asp Thr Arg Tyr Ser Pro Ser Phe 50 55 60 Gln Gly Gln Val Thr Ile Ser Ala Asp Arg Ser Ile Arg Thr Ala Tyr 65 70 75 80 Leu Gln Trp Ser Ser Leu Lys Ala Ser Asp Thr Ala Leu Tyr Tyr Cys 85 90 95 Ala Arg Thr Arg Glu Gly Tyr Phe Asp Tyr Trp Gly Gln Gly Thr Leu 100 105 110 Val Thr Val Ser Ser 115 <210> 600 <211> 117 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 600 Glu Val Gln Leu Val Gln Ser Gly Ala Glu Val Lys Lys Pro Gly Glu 1 5 10 15 Ser Leu Lys Ile Ser Cys Lys Gly Ser Gly Tyr Ser Phe Thr Asn Tyr 20 25 30 Trp Ile Ala Trp Val Arg Gln Met Pro Gly Lys Gly Leu Glu Trp Met 35 40 45 Gly Ile Ile Tyr Pro Gly Asp Ser Asp Thr Arg Tyr Ser Pro Ser Phe 50 55 60 Gln Gly Gln Val Thr Ile Ser Ala Asp Lys Ser Ile Arg Thr Ala Tyr 65 70 75 80 Leu Gln Trp Ser Ser Leu Lys Ala Ser Asp Thr Ala Met Tyr Tyr Cys 85 90 95 Ala Arg Thr Arg Glu Gly Tyr Phe Asp Tyr Trp Gly Gln Gly Thr Leu 100 105 110 Val Thr Val Ser Ser 115 <210> 601 <211> 117 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 601 Glu Val Gln Leu Val Gln Ser Gly Ala Asp Val Thr Lys Pro Gly Glu 1 5 10 15 Ser Leu Lys Ile Ser Cys Lys Val Ser Gly Tyr Arg Phe Thr Asn Tyr 20 25 30 Trp Ile Gly Trp Met Arg Gln Met Ser Gly Lys Gly Leu Glu Trp Met 35 40 45 Gly Ile Ile Tyr Pro Gly Asp Ser Asp Thr Arg Tyr Ser Pro Ser Phe 50 55 60 Gln Gly His Val Thr Ile Ser Ala Asp Lys Ser Ile Asn Thr Ala Tyr 65 70 75 80 Leu Arg Trp Ser Ser Leu Lys Ala Ser Asp Thr Ala Ile Tyr Tyr Cys 85 90 95 Ala Arg Thr Arg Glu Gly Phe Phe Asp Tyr Trp Gly Gln Gly Thr Pro 100 105 110 Val Thr Val Ser Ser 115 <210> 602 <211> 124 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 602 Gln Val Gln Leu Val Glu Ser Gly Gly Gly Val Val Gln Ser Gly Arg 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Arg Asn Tyr 20 25 30 Gly Met His Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ala Val Ile Trp Tyr Asp Gly Ser Asp Lys Tyr Tyr Ala Asp Ser Val 50 55 60 Arg Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 65 70 75 80 Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Asp Gly Tyr Asp Ile Leu Thr Gly Asn Pro Arg Asp Phe Asp 100 105 110 Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 115 120 <210> 603 <211> 119 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 603 Gln Val Gln Leu Lys Gln Ser Gly Pro Gly Leu Val Gln Pro Ser Gln 1 5 10 15 Ser Leu Ser Ile Thr Cys Thr Val Ser Gly Phe Ser Leu Thr Asn Tyr 20 25 30 Gly Val His Trp Val Arg Gln Ser Pro Gly Lys Gly Leu Glu Trp Leu 35 40 45 Gly Val Ile Trp Ser Gly Gly Asn Thr Asp Tyr Asn Thr Pro Phe Thr 50 55 60 Ser Arg Leu Ser Ile Asn Lys Asp Asn Ser Lys Ser Gln Val Phe Phe 65 70 75 80 Lys Met Asn Ser Leu Gln Ser Asn Asp Thr Ala Ile Tyr Tyr Cys Ala 85 90 95 Arg Ala Leu Thr Tyr Tyr Asp Tyr Glu Phe Ala Tyr Trp Gly Gln Gly 100 105 110 Thr Leu Val Thr Val Ser Ala 115 <210> 604 <211> 120 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 604 Gln Val Gln Leu Val Gln Ser Gly Ala Glu Val Lys Lys Pro Gly Ser 1 5 10 15 Ser Val Lys Val Ser Cys Lys Ala Ser Gly Phe Thr Phe Thr Asp Tyr 20 25 30 Lys Ile His Trp Val Arg Gln Ala Pro Gly Gln Gly Leu Glu Trp Met 35 40 45 Gly Tyr Phe Asn Pro Asn Ser Gly Tyr Ser Thr Tyr Ala Gln Lys Phe 50 55 60 Gln Gly Arg Val Thr Ile Thr Ala Asp Lys Ser Thr Ser Thr Ala Tyr 65 70 75 80 Met Glu Leu Ser Ser Leu Arg Ser Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Leu Ser Pro Gly Gly Tyr Tyr Val Met Asp Ala Trp Gly Gln 100 105 110 Gly Thr Thr Val Thr Val Ser Ser 115 120 <210> 605 <211> 125 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 605 Gln Val Gln Leu Val Glu Ser Gly Gly Gly Val Val Gln Pro Gly Arg 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Thr Tyr 20 25 30 Gly Met His Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ala Val Ile Trp Asp Asp Gly Ser Tyr Lys Tyr Tyr Gly Asp Ser Val 50 55 60 Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 65 70 75 80 Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Asp Gly Ile Thr Met Val Arg Gly Val Met Lys Asp Tyr Phe 100 105 110 Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 115 120 125 <210> 606 <211> 121 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 606 Gln Val Gln Leu Gln Glu Ser Gly Pro Gly Leu Val Lys Pro Ser Gln 1 5 10 15 Thr Leu Ser Leu Thr Cys Thr Val Ser Gly Gly Ser Ile Ser Ser Gly 20 25 30 Asp Tyr Tyr Trp Ser Trp Ile Arg Gln Pro Pro Gly Lys Gly Leu Glu 35 40 45 Trp Ile Gly Tyr Ile Tyr Tyr Ser Gly Ser Thr Asp Tyr Asn Pro Ser 50 55 60 Leu Lys Ser Arg Val Thr Met Ser Val Asp Thr Ser Lys Asn Gln Phe 65 70 75 80 Ser Leu Lys Val Asn Ser Val Thr Ala Ala Asp Thr Ala Val Tyr Tyr 85 90 95 Cys Ala Arg Val Ser Ile Phe Gly Val Gly Thr Phe Asp Tyr Trp Gly 100 105 110 Gln Gly Thr Leu Val Thr Val Ser Ser 115 120 <210> 607 <211> 121 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 607 Gln Val Gln Leu Val Gln Ser Gly Ala Glu Val Lys Lys Pro Gly Ser 1 5 10 15 Ser Val Lys Val Ser Cys Lys Ala Ser Gly Gly Thr Phe Ser Ser Tyr 20 25 30 Ala Ile Ser Trp Val Arg Gln Ala Pro Gly Gln Gly Leu Glu Trp Met 35 40 45 Gly Ser Ile Ile Pro Ile Phe Gly Thr Val Asn Tyr Ala Gln Lys Phe 50 55 60 Gln Gly Arg Val Thr Ile Thr Ala Asp Glu Ser Thr Ser Thr Ala Tyr 65 70 75 80 Met Glu Leu Ser Ser Leu Arg Ser Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Asp Pro Ser Val Asn Leu Tyr Trp Tyr Phe Asp Leu Trp Gly 100 105 110 Arg Gly Thr Leu Val Thr Val Ser Ser 115 120 <210> 608 <211> 119 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 608 Gln Val Gln Leu Val Gln Ser Gly Ala Glu Val Lys Lys Pro Gly Ser 1 5 10 15 Ser Val Lys Val Ser Cys Lys Ala Ser Gly Gly Thr Phe Gly Ser Tyr 20 25 30 Ala Ile Ser Trp Val Arg Gln Ala Pro Gly Gln Gly Leu Glu Trp Met 35 40 45 Gly Ser Ile Ile Pro Ile Phe Gly Ala Ala Asn Pro Ala Gln Lys Ser 50 55 60 Gln Gly Arg Val Thr Ile Thr Ala Asp Glu Ser Thr Ser Thr Ala Tyr 65 70 75 80 Met Glu Leu Ser Ser Leu Arg Ser Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Lys Met Gly Arg Gly Lys Val Ala Phe Asp Ile Trp Gly Gln Gly 100 105 110 Thr Met Val Thr Val Ser Ser 115 <210> 609 <211> 123 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 609 Gln Val Gln Leu Val Gln Ser Gly Ala Glu Val Lys Lys Pro Gly Ala 1 5 10 15 Ser Val Lys Val Ser Cys Lys Ala Ser Gly Tyr Ala Phe Thr Ser Tyr 20 25 30 Gly Ile Asn Trp Val Arg Gln Ala Pro Gly Gln Gly Leu Glu Trp Met 35 40 45 Gly Trp Ile Ser Ala Tyr Asn Gly Asn Thr Tyr Tyr Ala Gln Lys Leu 50 55 60 Arg Gly Arg Val Thr Met Thr Thr Asp Thr Ser Thr Ser Thr Ala Tyr 65 70 75 80 Met Glu Leu Arg Ser Leu Arg Ser Asp Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Asp Leu Gly Gly Tyr Gly Ser Gly Ser Val Pro Phe Asp Pro 100 105 110 Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser 115 120 <210> 610 <211> 123 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 610 Gln Val Gln Leu Gln Gln Ser Gly Ala Glu Val Lys Lys Pro Gly Ser 1 5 10 15 Ser Val Lys Val Ser Cys Lys Ala Ser Gly Tyr Thr Phe Thr Asn Tyr 20 25 30 Tyr Ile Tyr Trp Val Arg Gln Ala Pro Gly Gln Gly Leu Glu Trp Ile 35 40 45 Gly Gly Ile Asn Pro Thr Ser Gly Gly Ser Asn Phe Asn Glu Lys Phe 50 55 60 Lys Thr Arg Val Thr Ile Thr Ala Asp Glu Ser Ser Thr Thr Ala Tyr 65 70 75 80 Met Glu Leu Ser Ser Leu Arg Ser Glu Asp Thr Ala Phe Tyr Phe Cys 85 90 95 Thr Arg Gln Gly Leu Trp Phe Asp Ser Asp Gly Arg Gly Phe Asp Phe 100 105 110 Trp Gly Gln Gly Thr Thr Val Thr Val Ser Ser 115 120 <210> 611 <211> 119 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 611 Gln Val Gln Leu Gln Glu Ser Gly Pro Gly Leu Val Lys Pro Ser Glu 1 5 10 15 Thr Leu Ser Leu Thr Cys Thr Val Ser Gly Gly Ser Val Ser Ser Gly 20 25 30 Asp Tyr Tyr Trp Thr Trp Ile Arg Gln Ser Pro Gly Lys Gly Leu Glu 35 40 45 Trp Ile Gly His Ile Tyr Tyr Ser Gly Asn Thr Asn Tyr Asn Pro Ser 50 55 60 Leu Lys Ser Arg Leu Thr Ile Ser Ile Asp Thr Ser Lys Thr Gln Phe 65 70 75 80 Ser Leu Lys Leu Ser Ser Val Thr Ala Ala Asp Thr Ala Ile Tyr Tyr 85 90 95 Cys Val Arg Asp Arg Val Thr Gly Ala Phe Asp Ile Trp Gly Gln Gly 100 105 110 Thr Met Val Thr Val Ser Ser 115 <210> 612 <211> 118 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 612 Gln Ile Gln Leu Val Gln Ser Gly Pro Glu Leu Lys Lys Pro Gly Glu 1 5 10 15 Thr Val Lys Ile Ser Cys Lys Ala Ser Gly Tyr Thr Phe Thr Glu Tyr 20 25 30 Pro Ile His Trp Val Lys Gln Ala Pro Gly Lys Gly Phe Lys Trp Met 35 40 45 Gly Met Ile Tyr Thr Asp Ile Gly Lys Pro Thr Tyr Ala Glu Glu Phe 50 55 60 Lys Gly Arg Phe Ala Phe Ser Leu Glu Thr Ser Ala Ser Thr Ala Tyr 65 70 75 80 Leu Gln Ile Asn Asn Leu Lys Asn Glu Asp Thr Ala Thr Tyr Phe Cys 85 90 95 Val Arg Asp Arg Tyr Asp Ser Leu Phe Asp Tyr Trp Gly Gln Gly Thr 100 105 110 Thr Leu Thr Val Ser Ser 115 <210> 613 <211> 121 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 613 Glu Met Gln Leu Val Glu Ser Gly Gly Gly Phe Val Lys Pro Gly Gly 1 5 10 15 Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Ala Phe Ser His Tyr 20 25 30 Asp Met Ser Trp Val Arg Gln Thr Pro Lys Gln Arg Leu Glu Trp Val 35 40 45 Ala Tyr Ile Ala Ser Gly Gly Asp Ile Thr Tyr Tyr Ala Asp Thr Val 50 55 60 Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Gln Asn Thr Leu Tyr 65 70 75 80 Leu Gln Met Ser Ser Leu Lys Ser Glu Asp Thr Ala Met Phe Tyr Cys 85 90 95 Ser Arg Ser Ser Tyr Gly Asn Asn Gly Asp Ala Leu Asp Phe Trp Gly 100 105 110 Gln Gly Thr Ser Val Thr Val Ser Ser 115 120 <210> 614 <211> 119 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 614 Gln Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Ser Tyr 20 25 30 Ala Met Gly Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ser Ser Ile Ser Gly Ser Ser Arg Tyr Ile Tyr Tyr Ala Asp Ser Val 50 55 60 Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 65 70 75 80 Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Lys Met Asp Ala Ser Gly Ser Tyr Phe Asn Phe Trp Gly Gln Gly 100 105 110 Thr Leu Val Thr Val Ser Ser 115 <210> 615 <211> 115 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 615 Gln Val Gln Leu Leu Gln Ser Ala Ala Glu Val Lys Lys Pro Gly Glu 1 5 10 15 Ser Leu Lys Ile Ser Cys Lys Gly Ser Gly Tyr Ser Phe Thr Ser Tyr 20 25 30 Trp Ile Gly Trp Val Arg Gln Met Pro Gly Lys Gly Leu Glu Trp Met 35 40 45 Gly Ile Ile Tyr Pro Gly Asp Ser Asp Thr Arg Tyr Ser Pro Ser Phe 50 55 60 Gln Gly Gln Val Thr Ile Ser Ala Asp Lys Ser Ile Ser Thr Ala Tyr 65 70 75 80 Leu Gln Trp Ser Ser Leu Lys Ala Ser Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Trp Arg Asp Ser Pro Leu Trp Gly Gln Gly Thr Leu Val Thr 100 105 110 Val Ser Ser 115 <210> 616 <211> 120 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 616 Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Asn Ile Lys Asp Thr 20 25 30 Tyr Ile His Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ala Arg Ile Tyr Pro Thr Asn Gly Tyr Thr Arg Tyr Ala Asp Ser Val 50 55 60 Lys Gly Arg Phe Thr Ile Ser Ala Asp Thr Ser Lys Asn Thr Ala Tyr 65 70 75 80 Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ser Arg Trp Gly Gly Asp Gly Phe Tyr Ala Met Asp Tyr Trp Gly Gln 100 105 110 Gly Thr Leu Val Thr Val Ser Ser 115 120 <210> 617 <211> 120 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 617 Gln Val Gln Leu Gln Gln Ser Gly Pro Glu Leu Val Lys Pro Gly Ala 1 5 10 15 Ser Leu Lys Leu Ser Cys Thr Ala Ser Gly Phe Asn Ile Lys Asp Thr 20 25 30 Tyr Ile His Trp Val Lys Gln Arg Pro Glu Gln Gly Leu Glu Trp Ile 35 40 45 Gly Arg Ile Tyr Pro Thr Asn Gly Tyr Thr Arg Tyr Asp Pro Lys Phe 50 55 60 Gln Asp Lys Ala Thr Ile Thr Ala Asp Thr Ser Ser Asn Thr Ala Tyr 65 70 75 80 Leu Gln Val Ser Arg Leu Thr Ser Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ser Arg Trp Gly Gly Asp Gly Phe Tyr Ala Met Asp Tyr Trp Gly Gln 100 105 110 Gly Ala Ser Val Thr Val Ser Ser 115 120 <210> 618 <211> 119 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 618 Gln Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Arg Ser Tyr 20 25 30 Ala Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ser Ala Ile Ser Gly Arg Gly Asp Asn Thr Tyr Tyr Ala Asp Ser Val 50 55 60 Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 65 70 75 80 Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Lys Met Thr Ser Asn Ala Phe Ala Phe Asp Tyr Trp Gly Gln Gly 100 105 110 Thr Leu Val Thr Val Ser Ser 115 <210> 619 <211> 119 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 619 Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Thr Asp Tyr 20 25 30 Thr Met Asp Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ala Asp Val Asn Pro Asn Ser Gly Gly Ser Ile Tyr Asn Gln Arg Phe 50 55 60 Lys Gly Arg Phe Thr Leu Ser Val Asp Arg Ser Lys Asn Thr Leu Tyr 65 70 75 80 Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Asn Leu Gly Pro Ser Phe Tyr Phe Asp Tyr Trp Gly Gln Gly 100 105 110 Thr Leu Val Thr Val Ser Ser 115 <210> 620 <211> 119 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 620 Glu Val Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser His Tyr 20 25 30 Val Met Ala Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ser Ser Ile Ser Ser Ser Gly Gly Trp Thr Leu Tyr Ala Asp Ser Val 50 55 60 Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 65 70 75 80 Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Thr Arg Gly Leu Lys Met Ala Thr Ile Phe Asp Tyr Trp Gly Gln Gly 100 105 110 Thr Leu Val Thr Val Ser Ser 115 <210> 621 <211> 121 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 621 Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Leu Ser Gly Asp 20 25 30 Trp Ile His Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Gly Glu Ile Ser Ala Ala Gly Gly Tyr Thr Asp Tyr Ala Asp Ser Val 50 55 60 Lys Gly Arg Phe Thr Ile Ser Ala Asp Thr Ser Lys Asn Thr Ala Tyr 65 70 75 80 Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Glu Ser Arg Val Ser Phe Glu Ala Ala Met Asp Tyr Trp Gly 100 105 110 Gln Gly Thr Leu Val Thr Val Ser Ser 115 120 <210> 622 <211> 118 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 622 Gln Val Gln Leu Gln Glu Ser Gly Gly Gly Leu Val Lys Pro Gly Gly 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Ser Tyr 20 25 30 Trp Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ala Asn Ile Asn Arg Asp Gly Ser Ala Ser Tyr Tyr Val Asp Ser Val 50 55 60 Lys Gly Arg Phe Thr Ile Ser Arg Asp Asp Ala Lys Asn Ser Leu Tyr 65 70 75 80 Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Asp Arg Gly Val Gly Tyr Phe Asp Leu Trp Gly Arg Gly Thr 100 105 110 Leu Val Thr Val Ser Ser 115 <210> 623 <211> 129 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 623 Gln Val Gln Leu Val Gln Ser Gly Ala Glu Val Lys Lys Pro Gly Glu 1 5 10 15 Ser Leu Lys Ile Ser Cys Lys Gly Ser Gly Tyr Ser Phe Thr Ser Tyr 20 25 30 Trp Ile Ala Trp Val Arg Gln Met Pro Gly Lys Gly Leu Glu Tyr Met 35 40 45 Gly Leu Ile Tyr Pro Gly Asp Ser Asp Thr Lys Tyr Ser Pro Ser Phe 50 55 60 Gln Gly Gln Val Thr Ile Ser Val Asp Lys Ser Val Ser Thr Ala Tyr 65 70 75 80 Leu Gln Trp Ser Ser Leu Lys Pro Ser Asp Ser Ala Val Tyr Phe Cys 85 90 95 Ala Arg His Asp Val Gly Tyr Cys Thr Asp Arg Thr Cys Ala Lys Trp 100 105 110 Pro Glu Trp Leu Gly Val Trp Gly Gln Gly Thr Leu Val Thr Val Ser 115 120 125 Ser <210> 624 <211> 119 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 624 Glu Val Gln Leu Val Glu Ser Gly Gly Gly Val Val Gln Pro Gly Arg 1 5 10 15 Ser Leu Arg Leu Ser Cys Ser Thr Ser Gly Phe Thr Phe Ser Asp Tyr 20 25 30 Tyr Met Tyr Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ala Tyr Met Ser Asn Val Gly Ala Ile Thr Asp Tyr Pro Asp Thr Val 50 55 60 Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Phe 65 70 75 80 Leu Gln Met Asp Ser Leu Arg Pro Glu Asp Thr Gly Val Tyr Phe Cys 85 90 95 Ala Arg Gly Thr Arg Asp Gly Ser Trp Phe Ala Tyr Trp Gly Gln Gly 100 105 110 Thr Pro Val Thr Val Ser Ser 115 <210> 625 <211> 120 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 625 Gln Val Glu Leu Val Gln Ser Gly Ala Glu Val Lys Lys Pro Gly Glu 1 5 10 15 Ser Leu Lys Ile Ser Cys Lys Gly Ser Gly Tyr Ser Phe Thr Ser Tyr 20 25 30 Trp Ile Gly Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Met 35 40 45 Gly Ile Ile Asp Pro Gly Asp Ser Arg Thr Arg Tyr Ser Pro Ser Phe 50 55 60 Gln Gly Gln Val Thr Ile Ser Ala Asp Lys Ser Ile Ser Thr Ala Tyr 65 70 75 80 Leu Gln Trp Ser Ser Leu Lys Ala Ser Asp Thr Ala Met Tyr Tyr Cys 85 90 95 Ala Arg Gly Gln Leu Tyr Gly Gly Thr Tyr Met Asp Gly Trp Gly Gln 100 105 110 Gly Thr Leu Val Thr Val Ser Ser 115 120 <210> 626 <211> 119 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 626 Gln Val Gln Leu Gln Gln Ser Gly Pro Glu Leu Glu Lys Pro Gly Ala 1 5 10 15 Ser Val Lys Ile Ser Cys Lys Ala Ser Gly Tyr Ser Phe Thr Gly Tyr 20 25 30 Thr Met Asn Trp Val Lys Gln Ser His Gly Lys Ser Leu Glu Trp Ile 35 40 45 Gly Leu Ile Thr Pro Tyr Asn Gly Ala Ser Ser Tyr Asn Gln Lys Phe 50 55 60 Arg Gly Lys Ala Thr Leu Thr Val Asp Lys Ser Ser Ser Thr Ala Tyr 65 70 75 80 Met Asp Leu Leu Ser Leu Thr Ser Glu Asp Ser Ala Val Tyr Phe Cys 85 90 95 Ala Arg Gly Gly Tyr Asp Gly Arg Gly Phe Asp Tyr Trp Gly Gln Gly 100 105 110 Thr Thr Val Thr Val Ser Ser 115 <210> 627 <211> 122 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 627 Gln Val Tyr Leu Val Glu Ser Gly Gly Gly Val Val Gln Pro Gly Arg 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Ile Thr Phe Ser Ile Tyr 20 25 30 Gly Met His Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ala Val Ile Trp Tyr Asp Gly Ser His Glu Tyr Tyr Ala Asp Ser Val 50 55 60 Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 65 70 75 80 Leu Leu Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Asp Gly Asp Tyr Tyr Asp Ser Gly Ser Pro Leu Asp Tyr Trp 100 105 110 Gly Gln Gly Thr Leu Val Thr Val Ser Ser 115 120 <210> 628 <211> 122 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 628 Gln Val His Leu Val Glu Ser Gly Gly Gly Val Val Gln Pro Gly Arg 1 5 10 15 Ser Leu Arg Leu Ser Cys Val Ala Ser Gly Ile Thr Phe Arg Ile Tyr 20 25 30 Gly Met His Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ala Val Leu Trp Tyr Asp Gly Ser His Glu Tyr Tyr Ala Asp Ser Val 50 55 60 Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 65 70 75 80 Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Ile Tyr Tyr Cys 85 90 95 Ala Arg Asp Gly Asp Tyr Tyr Asp Ser Gly Ser Pro Leu Asp Tyr Trp 100 105 110 Gly Gln Gly Thr Leu Val Thr Val Ser Ser 115 120 <210> 629 <211> 131 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 629 Glu Val His Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Arg Tyr 20 25 30 Trp Met Ser Trp Val Arg Gln Ala Gln Gly Lys Gly Leu Glu Trp Val 35 40 45 Ala Ser Ile Lys Gln Ala Gly Ser Glu Lys Thr Tyr Val Asp Ser Val 50 55 60 Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Ser Leu Ser 65 70 75 80 Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Glu Gly Ala Tyr Tyr Tyr Asp Ser Ala Ser Tyr Tyr Pro Tyr 100 105 110 Tyr Tyr Tyr Tyr Ser Met Asp Val Trp Gly Gln Gly Thr Thr Val Thr 115 120 125 Val Ser Ser 130 <210> 630 <211> 119 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 630 Gln Val Gln Leu Gln Gln Ser Gly Pro Glu Leu Glu Lys Pro Gly Ala 1 5 10 15 Ser Val Lys Ile Ser Cys Lys Ala Ser Gly Tyr Ser Phe Thr Gly Tyr 20 25 30 Thr Met Asn Trp Val Lys Gln Ser His Gly Lys Ser Leu Glu Trp Ile 35 40 45 Gly Leu Ile Thr Pro Tyr Asn Gly Ala Ser Ser Tyr Asn Gln Lys Phe 50 55 60 Arg Gly Lys Ala Thr Leu Thr Val Asp Lys Ser Ser Ser Thr Ala Tyr 65 70 75 80 Met Asp Leu Leu Ser Leu Thr Ser Glu Asp Ser Ala Val Tyr Phe Cys 85 90 95 Ala Arg Gly Gly Tyr Asp Gly Arg Gly Phe Asp Tyr Trp Gly Ser Gly 100 105 110 Thr Pro Val Thr Val Ser Ser 115 <210> 631 <211> 119 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 631 Glu Val Gln Leu Gln Glu Ser Gly Pro Glu Leu Val Lys Pro Gly Ala 1 5 10 15 Ser Val Lys Met Ser Cys Lys Ala Ser Gly Tyr Thr Phe Pro Ser Tyr 20 25 30 Val Leu His Trp Val Lys Gln Lys Pro Gly Gln Gly Leu Glu Trp Ile 35 40 45 Gly Tyr Ile Asn Pro Tyr Asn Asp Gly Thr Gln Tyr Asn Glu Lys Phe 50 55 60 Lys Gly Lys Ala Thr Leu Thr Ser Asp Lys Ser Ser Ser Thr Ala Tyr 65 70 75 80 Met Glu Leu Ser Arg Leu Thr Ser Glu Asp Ser Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Gly Phe Gly Gly Ser Tyr Gly Phe Ala Tyr Trp Gly Gln Gly 100 105 110 Thr Leu Ile Thr Val Ser Ala 115 <210> 632 <211> 119 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 632 Gln Val Gln Leu Gln Gln Ser Gly Ala Glu Val Lys Lys Phe Gly Ala 1 5 10 15 Ser Val Lys Val Ser Cys Glu Ala Ser Gly Tyr Thr Phe Pro Ser Tyr 20 25 30 Val Leu His Trp Val Lys Gln Ala Pro Gly Gln Gly Leu Glu Trp Ile 35 40 45 Gly Tyr Ile Asn Pro Tyr Asn Asp Gly Thr Gln Thr Asn Lys Lys Phe 50 55 60 Lys Gly Lys Ala Thr Leu Thr Arg Asp Thr Ser Ile Asn Thr Ala Tyr 65 70 75 80 Met Glu Leu Ser Arg Leu Arg Ser Asp Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Gly Phe Gly Gly Ser Tyr Gly Phe Ala Tyr Asn Gly Gln Gly 100 105 110 Thr Leu Val Thr Val Ser Ser 115 <210> 633 <211> 118 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 633 Gln Val Gln Leu Gln Gln Ser Gly Ala Glu Leu Met Lys Pro Gly Ala 1 5 10 15 Ser Val Lys Ile Ser Cys Lys Ala Thr Gly Tyr Thr Phe Ser Ala Tyr 20 25 30 Trp Ile Glu Trp Val Lys Gln Arg Pro Gly His Gly Leu Glu Trp Ile 35 40 45 Gly Glu Ile Leu Pro Gly Ser Asn Asn Ser Arg Tyr Asn Glu Lys Phe 50 55 60 Lys Gly Lys Ala Thr Phe Thr Ala Asp Thr Ser Ser Asn Thr Ala Tyr 65 70 75 80 Met Gln Leu Ser Ser Leu Thr Ser Glu Asp Ser Ala Val Tyr Tyr Cys 85 90 95 Ser Arg Ser Tyr Asp Phe Ala Trp Phe Ala Tyr Trp Gly Gln Gly Thr 100 105 110 Pro Val Thr Val Ser Ala 115 <210> 634 <211> 118 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 634 Gln Val Gln Leu Val Gln Ser Gly Ala Glu Val Lys Lys Pro Gly Ala 1 5 10 15 Ser Val Lys Val Ser Cys Lys Ala Ser Gly Tyr Thr Phe Ser Ala Tyr 20 25 30 Trp Ile Glu Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Gly Glu Ile Leu Pro Gly Ser Asn Asn Ser Arg Tyr Asn Glu Lys Phe 50 55 60 Lys Gly Arg Val Thr Val Thr Arg Asp Thr Ser Thr Asn Thr Ala Tyr 65 70 75 80 Met Glu Leu Ser Ser Leu Arg Ser Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Ser Tyr Asp Phe Ala Trp Phe Ala Tyr Trp Gly Gln Gly Thr 100 105 110 Leu Val Thr Val Ser Ser 115 <210> 635 <211> 123 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 635 Gln Val Gln Leu Val Gln Ser Gly Ala Glu Val Lys Lys Pro Gly Ser 1 5 10 15 Ser Val Lys Val Ser Cys Lys Thr Ser Gly Asp Thr Phe Ser Thr Tyr 20 25 30 Ala Ile Ser Trp Val Arg Gln Ala Pro Gly Gln Gly Leu Glu Trp Met 35 40 45 Gly Gly Ile Ile Pro Ile Phe Gly Lys Ala His Tyr Ala Gln Lys Phe 50 55 60 Gln Gly Arg Val Thr Ile Thr Ala Asp Glu Ser Thr Ser Thr Ala Tyr 65 70 75 80 Met Glu Leu Ser Ser Leu Arg Ser Glu Asp Thr Ala Val Tyr Phe Cys 85 90 95 Ala Arg Lys Phe His Phe Val Ser Gly Ser Pro Phe Gly Met Asp Val 100 105 110 Trp Gly Gln Gly Thr Thr Val Thr Val Ser Ser 115 120 <210> 636 <211> 121 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 636 Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Arg Tyr 20 25 30 Trp Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ala Asn Ile Lys Gln Asp Gly Ser Glu Lys Tyr Tyr Val Asp Ser Val 50 55 60 Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Ser Leu Tyr 65 70 75 80 Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Glu Gly Gly Trp Phe Gly Glu Leu Ala Phe Asp Tyr Trp Gly 100 105 110 Gln Gly Thr Leu Val Thr Val Ser Ser 115 120 <210> 637 <211> 118 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 637 Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Asp Ser 20 25 30 Trp Ile His Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ala Trp Ile Ser Pro Tyr Gly Gly Ser Thr Tyr Tyr Ala Asp Ser Val 50 55 60 Lys Gly Arg Phe Thr Ile Ser Ala Asp Thr Ser Lys Asn Thr Ala Tyr 65 70 75 80 Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Arg His Trp Pro Gly Gly Phe Asp Tyr Trp Gly Gln Gly Thr 100 105 110 Leu Val Thr Val Ser Ser 115 <210> 638 <211> 120 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 638 Glu Val Gln Leu Leu Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Ser Tyr 20 25 30 Ile Met Met Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ser Ser Ile Tyr Pro Ser Gly Gly Ile Thr Phe Tyr Ala Asp Thr Val 50 55 60 Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr 65 70 75 80 Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Ile Lys Leu Gly Thr Val Thr Thr Val Asp Tyr Trp Gly Gln 100 105 110 Gly Thr Leu Val Thr Val Ser Ser 115 120 <210> 639 <211> 115 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 639 Glu Val Gln Leu Val Gln Ser Gly Pro Glu Val Lys Lys Pro Gly Ala 1 5 10 15 Thr Val Lys Ile Ser Cys Lys Thr Ser Gly Tyr Thr Phe Thr Glu Tyr 20 25 30 Thr Ile His Trp Val Lys Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile 35 40 45 Gly Asn Ile Asn Pro Asn Asn Gly Gly Thr Thr Tyr Asn Gln Lys Phe 50 55 60 Glu Asp Lys Ala Thr Leu Thr Val Asp Lys Ser Thr Asp Thr Ala Tyr 65 70 75 80 Met Glu Leu Ser Ser Leu Arg Ser Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Ala Gly Trp Asn Phe Asp Tyr Trp Gly Gln Gly Thr Leu Leu Thr 100 105 110 Val Ser Ser 115 <210> 640 <211> 121 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 640 Gln Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Lys Pro Gly Glu 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Asp Tyr 20 25 30 Tyr Met Tyr Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ala Ile Ile Ser Asp Gly Gly Tyr Tyr Thr Tyr Tyr Ser Asp Ile Ile 50 55 60 Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Ser Leu Tyr 65 70 75 80 Leu Gln Met Asn Ser Leu Lys Ala Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Gly Phe Pro Leu Leu Arg His Gly Ala Met Asp Tyr Trp Gly 100 105 110 Gln Gly Thr Leu Val Thr Val Ser Ser 115 120 <210> 641 <211> 121 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 641 Gln Glu Gln Leu Val Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Gly 1 5 10 15 Ser Leu Thr Leu Ser Cys Lys Ala Ser Gly Phe Asp Phe Ser Ala Tyr 20 25 30 Tyr Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile 35 40 45 Ala Thr Ile Tyr Pro Ser Ser Gly Lys Thr Tyr Tyr Ala Thr Trp Val 50 55 60 Asn Gly Arg Phe Thr Ile Ser Ser Asp Asn Ala Gln Asn Thr Val Asp 65 70 75 80 Leu Gln Met Asn Ser Leu Thr Ala Ala Asp Arg Ala Thr Tyr Phe Cys 85 90 95 Ala Arg Asp Ser Tyr Ala Asp Asp Gly Ala Leu Phe Asn Ile Trp Gly 100 105 110 Pro Gly Thr Leu Val Thr Ile Ser Ser 115 120 <210> 642 <211> 119 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 642 Glu Val Lys Leu Val Glu Ser Gly Gly Gly Leu Val Lys Pro Gly Gly 1 5 10 15 Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Ser Tyr 20 25 30 Ala Met Ser Trp Val Arg Gln Ile Pro Glu Lys Arg Leu Glu Trp Val 35 40 45 Ala Ser Ile Ser Arg Gly Gly Thr Thr Tyr Tyr Pro Asp Ser Val Lys 50 55 60 Gly Arg Phe Thr Ile Ser Arg Asp Asn Val Arg Asn Ile Leu Tyr Leu 65 70 75 80 Gln Met Ser Ser Leu Arg Ser Glu Asp Thr Ala Met Tyr Tyr Cys Gly 85 90 95 Arg Tyr Asp Tyr Asp Gly Tyr Tyr Ala Met Asp Tyr Trp Gly Gln Gly 100 105 110 Thr Ser Val Thr Val Ser Ser 115 <210> 643 <211> 117 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 643 Gln Ser Leu Glu Glu Ser Gly Gly Arg Leu Val Thr Pro Gly Thr Pro 1 5 10 15 Leu Thr Leu Thr Cys Thr Val Ser Gly Ile Asp Leu Asn Ser His Trp 20 25 30 Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile Gly 35 40 45 Ile Ile Ala Ala Ser Gly Ser Thr Tyr Tyr Ala Asn Trp Ala Lys Gly 50 55 60 Arg Phe Thr Ile Ser Lys Thr Ser Thr Thr Val Asp Leu Arg Ile Ala 65 70 75 80 Ser Pro Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys Ala Arg Asp Tyr 85 90 95 Gly Asp Tyr Arg Leu Val Thr Phe Asn Ile Trp Gly Pro Gly Thr Leu 100 105 110 Val Thr Val Ser Ser 115 <210> 644 <211> 116 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 644 Gln Ser Val Lys Glu Ser Glu Gly Asp Leu Val Thr Pro Ala Gly Asn 1 5 10 15 Leu Thr Leu Thr Cys Thr Ala Ser Gly Ser Asp Ile Asn Asp Tyr Pro 20 25 30 Ile Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Ile Gly 35 40 45 Phe Ile Asn Ser Gly Gly Ser Thr Trp Tyr Ala Ser Trp Val Lys Gly 50 55 60 Arg Phe Thr Ile Ser Arg Thr Ser Thr Thr Val Asp Leu Lys Met Thr 65 70 75 80 Ser Leu Thr Thr Asp Asp Thr Ala Thr Tyr Phe Cys Ala Arg Gly Tyr 85 90 95 Ser Thr Tyr Tyr Cys Asp Phe Asn Ile Trp Gly Pro Gly Thr Leu Val 100 105 110 Thr Ile Ser Ser 115 <210> 645 <211> 115 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 645 Gln Val Gln Leu Val Gln Ser Gly Ala Glu Val Val Lys Pro Gly Ala 1 5 10 15 Ser Val Lys Ile Ser Cys Lys Ala Ser Gly Tyr Thr Phe Thr Asp His 20 25 30 Ala Ile His Trp Val Lys Gln Asn Pro Gly Gln Arg Leu Glu Trp Ile 35 40 45 Gly Tyr Phe Ser Pro Gly Asn Asp Asp Phe Lys Tyr Asn Glu Arg Phe 50 55 60 Lys Gly Lys Ala Thr Leu Thr Ala Asp Thr Ser Ala Ser Thr Ala Tyr 65 70 75 80 Val Glu Leu Ser Ser Leu Arg Ser Glu Asp Thr Ala Val Tyr Phe Cys 85 90 95 Thr Arg Ser Leu Asn Met Ala Tyr Trp Gly Gln Gly Thr Leu Val Thr 100 105 110 Val Ser Ser 115 <210> 646 <211> 119 <212> PRT <213> artificial sequence <220> <223> synthetic <220> <221> MISC_FEATURE <222> (68)..(68) <223> X is any amino acid <400> 646 Gln Ile Gln Leu Val Gln Ser Gly Pro Glu Leu Lys Lys Pro Gly Glu 1 5 10 15 Thr Val Lys Ile Ser Cys Lys Ala Ser Gly Tyr Thr Phe Thr Asn Phe 20 25 30 Gly Met Asn Trp Val Lys Gln Gly Pro Gly Glu Gly Leu Lys Trp Met 35 40 45 Gly Trp Ile Asn Thr Asn Thr Gly Glu Pro Arg Tyr Ala Glu Glu Phe 50 55 60 Lys Gly Arg Xaa Ala Phe Ser Leu Glu Thr Thr Ala Ser Thr Ala Tyr 65 70 75 80 Leu Gln Ile Asn Asn Leu Lys Asn Glu Asp Thr Ala Thr Tyr Phe Cys 85 90 95 Ala Arg Asp Trp Asp Gly Ala Tyr Phe Phe Asp Tyr Trp Gly Gln Gly 100 105 110 Thr Thr Leu Thr Val Ser Ser 115 <210> 647 <211> 117 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 647 Gln Val Gln Leu Gln Gln Ser Arg Pro Glu Leu Val Lys Pro Gly Ala 1 5 10 15 Ser Val Lys Met Ser Cys Lys Ala Ser Gly Tyr Thr Phe Thr Asp Tyr 20 25 30 Val Ile Ser Trp Val Lys Gln Arg Thr Gly Gln Gly Leu Glu Trp Ile 35 40 45 Gly Glu Ile Tyr Pro Gly Ser Asn Ser Ile Tyr Tyr Asn Glu Lys Phe 50 55 60 Lys Gly Arg Ala Thr Leu Thr Ala Asp Lys Ser Ser Ser Thr Ala Tyr 65 70 75 80 Met Gln Leu Ser Ser Leu Thr Ser Glu Asp Ser Ala Val Tyr Phe Cys 85 90 95 Ala Met Gly Gly Asn Tyr Gly Phe Asp Tyr Trp Gly Gln Gly Thr Thr 100 105 110 Leu Thr Val Ser Ser 115 <210> 648 <211> 122 <212> PRT <213> artificial sequence <220> <223> synthetic <220> <221> MISC_FEATURE <222> (97)..(97) <223> X is any amino acid <400> 648 Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Lys Gly 1 5 10 15 Ser Leu Lys Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Asn Thr Tyr 20 25 30 Ala Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ala Arg Ile Arg Ser Lys Ser Asn Asn Tyr Ala Thr Tyr Tyr Ala Asp 50 55 60 Ser Val Lys Asp Arg Phe Thr Ile Ser Arg Asp Asp Ser Gln Ser Met 65 70 75 80 Leu Tyr Leu Gln Met Asn Asn Leu Lys Thr Glu Asp Thr Ala Met Tyr 85 90 95 Xaa Cys Val Arg Gln Trp Asp Tyr Asp Val Arg Ala Met Asn Tyr Trp 100 105 110 Gly Gln Gly Thr Ser Val Thr Val Ser Ser 115 120 <210> 649 <211> 121 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 649 Gln Val Gln Leu Gln Gln Ser Gly Ser Glu Leu Lys Lys Pro Gly Ala 1 5 10 15 Ser Val Lys Val Ser Cys Lys Ala Ser Gly Tyr Thr Phe Thr Asn Tyr 20 25 30 Gly Met Asn Trp Val Lys Gln Ala Pro Gly Gln Gly Leu Lys Trp Met 35 40 45 Gly Trp Ile Asn Thr Tyr Thr Gly Glu Pro Thr Tyr Thr Asp Asp Phe 50 55 60 Lys Gly Arg Phe Ala Phe Ser Leu Asp Thr Ser Val Ser Thr Ala Tyr 65 70 75 80 Leu Gln Ile Ser Ser Leu Lys Ala Asp Asp Thr Ala Val Tyr Phe Cys 85 90 95 Ala Arg Gly Gly Phe Gly Ser Ser Tyr Trp Tyr Phe Asp Val Trp Gly 100 105 110 Gln Gly Ser Leu Val Thr Val Ser Ser 115 120 <210> 650 <211> 126 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 650 Gln Ala Gln Val Val Glu Ser Gly Gly Gly Val Val Gln Ser Gly Arg 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Ala Phe Ser Ser Ser Tyr 20 25 30 Gly Met His Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ala Val Ile Trp Tyr Asp Gly Ser Asn Lys Tyr Tyr Ala Asp Ser Val 50 55 60 Arg Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Glu Asn Thr Leu Tyr 65 70 75 80 Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Asp His Tyr Gly Ser Gly Val His Tyr Phe Tyr Tyr Gly 100 105 110 Leu Asp Val Trp Gly Gln Gly Thr Thr Val Thr Val Ser Ser 115 120 125 <210> 651 <211> 117 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 651 Glu Val Gln Leu Val Gln Ser Gly Gly Gly Leu Val Lys Pro Gly Gly 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Ser Tyr 20 25 30 Ser Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ser Ser Ile Ser Ser Ser Ser Ser Tyr Ile Tyr Tyr Ala Asp Ser Val 50 55 60 Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Ser Leu Tyr 65 70 75 80 Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Ala Arg Val Thr Asp Ala Phe Asp Ile Trp Gly Gln Gly Thr Met Val 100 105 110 Thr Val Ser Ser Ala 115 <210> 652 <211> 117 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 652 Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly 1 5 10 15 Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Ser Tyr 20 25 30 Gly Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val 35 40 45 Ala Thr Ile Thr Ser Gly Gly Ser Tyr Thr Tyr Tyr Val Asp Ser Val 50 55 60 Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ala Lys Asn Thr Leu Tyr 65 70 75 80 Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys 85 90 95 Val Arg Ile Gly Glu Asp Ala Leu Asp Tyr Trp Gly Gln Gly Thr Leu 100 105 110 Val Thr Val Ser Ser 115 <210> 653 <211> 118 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 653 Lys Val Gln Leu Gln Gln Ser Gly Thr Glu Leu Val Lys Pro Gly Ala 1 5 10 15 Ser Val Lys Val Ser Cys Lys Ala Ser Gly Tyr Ile Phe Thr Glu Tyr 20 25 30 Ile Ile His Trp Val Lys Gln Arg Ser Gly Gln Gly Leu Glu Trp Ile 35 40 45 Gly Trp Leu Tyr Pro Glu Ser Asn Ile Ile Lys Tyr Asn Glu Lys Phe 50 55 60 Lys Asp Lys Ala Thr Leu Thr Ala Asp Lys Ser Ser Ser Thr Val Tyr 65 70 75 80 Met Glu Leu Ser Arg Leu Thr Ser Glu Asp Ser Ala Val Tyr Phe Cys 85 90 95 Thr Arg His Asp Gly Thr Asn Phe Asp Tyr Trp Gly Gln Gly Thr Thr 100 105 110 Leu Thr Val Ser Ser Ala 115 <210> 654 <211> 106 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 654 Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Lys Thr Ser Gln Asp Ile Asn Lys Tyr 20 25 30 Met Ala Trp Tyr Gln Gln Thr Pro Gly Lys Ala Pro Arg Leu Leu Ile 35 40 45 His Tyr Thr Ser Ala Leu Gln Pro Gly Ile Pro Ser Arg Phe Ser Gly 50 55 60 Ser Gly Ser Gly Arg Asp Tyr Thr Phe Thr Ile Ser Ser Leu Gln Pro 65 70 75 80 Glu Asp Ile Ala Thr Tyr Tyr Cys Leu Gln Tyr Asp Asn Leu Trp Thr 85 90 95 Phe Gly Gln Gly Thr Lys Val Glu Ile Lys 100 105 <210> 655 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 655 Glu Ile Val Leu Thr Gln Ser Pro Gly Thr Leu Ser Leu Ser Pro Gly 1 5 10 15 Glu Arg Ala Thr Leu Ser Cys Arg Ala Ser Gln Ser Val Ser Ser Thr 20 25 30 Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln Ala Pro Arg Leu Leu 35 40 45 Ile Tyr Gly Ala Ser Ser Arg Ala Thr Gly Ile Pro Asp Arg Phe Ser 50 55 60 Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Arg Leu Glu 65 70 75 80 Pro Glu Asp Phe Ala Val Tyr Tyr Cys Gln His Tyr Asp Asn Ser Gln 85 90 95 Thr Phe Gly Gln Gly Thr Lys Val Glu Ile Lys 100 105 <210> 656 <211> 106 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 656 Glu Asn Val Leu Thr Gln Ser Pro Ser Ser Met Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Asn Ile Ala Cys Ser Ala Ser Ser Ser Val Ser Tyr Met 20 25 30 His Trp Phe Gln Gln Lys Pro Gly Lys Ser Pro Lys Leu Trp Ile Tyr 35 40 45 Ser Thr Ser Asn Leu Ala Ser Gly Val Pro Ser Arg Phe Ser Gly Ser 50 55 60 Gly Ser Gly Thr Asp Tyr Ser Leu Thr Ile Ser Ser Met Gln Pro Glu 65 70 75 80 Asp Ala Ala Thr Tyr Tyr Cys Gln Gln Arg Ser Ser Tyr Pro Leu Thr 85 90 95 Phe Gly Gly Gly Thr Lys Leu Glu Ile Lys 100 105 <210> 657 <211> 111 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 657 Asp Ile Gln Leu Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Arg Ala Gly Glu Ser Val Asp Ile Phe 20 25 30 Gly Val Gly Phe Leu His Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro 35 40 45 Lys Leu Leu Ile Tyr Arg Ala Ser Asn Leu Glu Ser Gly Val Pro Ser 50 55 60 Arg Phe Ser Gly Ser Gly Ser Arg Thr Asp Phe Thr Leu Thr Ile Ser 65 70 75 80 Ser Leu Gln Pro Glu Asp Phe Ala Thr Tyr Tyr Cys Gln Gln Thr Asn 85 90 95 Glu Asp Pro Tyr Thr Phe Gly Gln Gly Thr Lys Val Glu Ile Lys 100 105 110 <210> 658 <211> 111 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 658 Asp Ile Gln Leu Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Arg Ala Gly Glu Ser Val Asp Ile Phe 20 25 30 Gly Val Gly Phe Leu His Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro 35 40 45 Lys Leu Leu Ile Tyr Arg Ala Ser Asn Leu Glu Ser Gly Val Pro Ser 50 55 60 Arg Phe Ser Gly Ser Gly Ser Arg Thr Asp Phe Thr Leu Thr Ile Ser 65 70 75 80 Ser Leu Gln Pro Glu Asp Phe Ala Thr Tyr Tyr Cys Gln Gln Thr Asn 85 90 95 Glu Asp Pro Tyr Thr Phe Gly Gln Gly Thr Lys Val Glu Ile Lys 100 105 110 <210> 659 <211> 106 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 659 Asp Ile Gln Leu Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Lys Ala Ser Gln Asp Val Gly Thr Ser 20 25 30 Val Ala Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile 35 40 45 Tyr Trp Thr Ser Thr Arg His Thr Gly Val Pro Ser Arg Phe Ser Gly 50 55 60 Ser Gly Ser Gly Thr Asp Phe Thr Phe Thr Ile Ser Ser Leu Gln Pro 65 70 75 80 Glu Asp Ile Ala Thr Tyr Tyr Cys Gln Gln Tyr Ser Leu Tyr Arg Ser 85 90 95 Phe Gly Gln Gly Thr Lys Val Glu Ile Lys 100 105 <210> 660 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 660 Gln Thr Val Leu Ser Gln Ser Pro Ala Ile Leu Ser Ala Ser Pro Gly 1 5 10 15 Glu Lys Val Thr Met Thr Cys Arg Ala Ser Ser Ser Val Thr Tyr Ile 20 25 30 His Trp Tyr Gln Gln Lys Pro Gly Ser Ser Pro Lys Ser Trp Ile Tyr 35 40 45 Ala Thr Ser Asn Leu Ala Ser Gly Val Pro Ala Arg Phe Ser Gly Ser 50 55 60 Gly Ser Gly Thr Ser Tyr Ser Leu Thr Ile Ser Arg Val Glu Ala Glu 65 70 75 80 Asp Ala Ala Thr Tyr Tyr Cys Gln His Trp Ser Ser Lys Pro Pro Thr 85 90 95 Phe Gly Gly Gly Thr Lys Leu Glu Ile Lys Arg 100 105 <210> 661 <211> 116 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 661 Gln Ala Val Leu Thr Gln Pro Ala Ser Leu Ser Ala Ser Pro Gly Ala 1 5 10 15 Ser Ala Ser Leu Thr Cys Thr Leu Arg Arg Gly Ile Asn Val Gly Ala 20 25 30 Tyr Ser Ile Tyr Trp Tyr Gln Gln Lys Pro Gly Ser Pro Pro Gln Tyr 35 40 45 Leu Leu Arg Tyr Lys Ser Asp Ser Asp Lys Gln Gln Gly Ser Gly Val 50 55 60 Ser Ser Arg Phe Ser Ala Ser Lys Asp Ala Ser Ala Asn Ala Gly Ile 65 70 75 80 Leu Leu Ile Ser Gly Leu Gln Ser Glu Asp Glu Ala Asp Tyr Tyr Cys 85 90 95 Met Ile Trp His Ser Gly Ala Ser Ala Val Phe Gly Gly Gly Thr Lys 100 105 110 Leu Thr Val Leu 115 <210> 662 <211> 111 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 662 Asp Ile Gln Leu Thr Gln Ser Pro Ala Ser Leu Ala Val Ser Leu Gly 1 5 10 15 Gln Arg Ala Thr Ile Ser Cys Lys Ala Ser Gln Ser Val Asp Tyr Asp 20 25 30 Gly Asp Ser Tyr Leu Asn Trp Tyr Gln Gln Ile Pro Gly Gln Pro Pro 35 40 45 Lys Leu Leu Ile Tyr Asp Ala Ser Asn Leu Val Ser Gly Ile Pro Pro 50 55 60 Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Asn Ile His 65 70 75 80 Pro Val Glu Lys Val Asp Ala Ala Thr Tyr His Cys Gln Gln Ser Thr 85 90 95 Glu Asp Pro Trp Thr Phe Gly Gly Gly Thr Lys Leu Glu Ile Lys 100 105 110 <210> 663 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 663 Glu Ile Val Leu Thr Gln Ser Pro Ala Thr Leu Ser Leu Ser Pro Gly 1 5 10 15 Glu Arg Ala Thr Leu Ser Cys Arg Ala Ser Gln Ser Val Ser Ser Tyr 20 25 30 Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln Ala Pro Arg Leu Leu Ile 35 40 45 Tyr Asp Ala Ser Asn Arg Ala Thr Gly Ile Pro Ala Arg Phe Ser Gly 50 55 60 Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Glu Pro 65 70 75 80 Glu Asp Phe Ala Val Tyr Tyr Cys Gln Gln Arg Ser Asn Trp Pro Ile 85 90 95 Thr Phe Gly Gln Gly Thr Arg Leu Glu Ile Lys 100 105 <210> 664 <211> 106 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 664 Gln Ile Val Leu Ser Gln Ser Pro Ala Ile Leu Ser Ala Ser Pro Gly 1 5 10 15 Glu Lys Val Thr Met Thr Cys Arg Ala Ser Ser Ser Val Ser Tyr Met 20 25 30 His Trp Tyr Gln Gln Lys Pro Gly Ser Ser Pro Lys Pro Trp Ile Tyr 35 40 45 Ala Pro Ser Asn Leu Ala Ser Gly Val Pro Ala Arg Phe Ser Gly Ser 50 55 60 Gly Ser Gly Thr Ser Tyr Ser Leu Thr Ile Ser Arg Val Glu Ala Glu 65 70 75 80 Asp Ala Ala Thr Tyr Tyr Cys Gln Gln Trp Ser Phe Asn Pro Pro Thr 85 90 95 Phe Gly Ala Gly Thr Lys Leu Glu Leu Lys 100 105 <210> 665 <211> 112 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 665 Asp Ile Val Met Thr Gln Thr Pro Leu Ser Leu Pro Val Thr Pro Gly 1 5 10 15 Glu Pro Ala Ser Ile Ser Cys Arg Ser Ser Lys Ser Leu Leu His Ser 20 25 30 Asn Gly Ile Thr Tyr Leu Tyr Trp Tyr Leu Gln Lys Pro Gly Gln Ser 35 40 45 Pro Gln Leu Leu Ile Tyr Gln Met Ser Asn Leu Val Ser Gly Val Pro 50 55 60 Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Lys Ile 65 70 75 80 Ser Arg Val Glu Ala Glu Asp Val Gly Val Tyr Tyr Cys Ala Gln Asn 85 90 95 Leu Glu Leu Pro Tyr Thr Phe Gly Gly Gly Thr Lys Val Glu Ile Lys 100 105 110 <210> 666 <211> 106 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 666 Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Arg Ala Ser Ser Ser Val Ser Tyr Met 20 25 30 His Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Pro Leu Ile Tyr 35 40 45 Ala Pro Ser Asn Leu Ala Ser Gly Val Pro Ser Arg Phe Ser Gly Ser 50 55 60 Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln Pro Glu 65 70 75 80 Asp Phe Ala Thr Tyr Tyr Cys Gln Gln Trp Ser Phe Asn Pro Pro Thr 85 90 95 Phe Gly Gln Gly Thr Lys Val Glu Ile Lys 100 105 <210> 667 <211> 106 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 667 Gln Ile Val Leu Ser Gln Ser Pro Ala Ile Leu Ser Ala Ser Pro Gly 1 5 10 15 Glu Lys Val Thr Met Thr Cys Arg Ala Ser Ser Ser Val Ser Tyr Ile 20 25 30 His Trp Phe Gln Gln Lys Pro Gly Ser Ser Pro Lys Pro Trp Ile Tyr 35 40 45 Ala Thr Ser Asn Leu Ala Ser Gly Val Pro Val Arg Phe Ser Gly Ser 50 55 60 Gly Ser Gly Thr Ser Tyr Ser Leu Thr Ile Ser Arg Val Glu Ala Glu 65 70 75 80 Asp Ala Ala Thr Tyr Tyr Cys Gln Gln Trp Thr Ser Asn Pro Pro Thr 85 90 95 Phe Gly Gly Gly Thr Lys Leu Glu Ile Lys 100 105 <210> 668 <211> 106 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 668 Gln Ile Val Leu Ser Gln Ser Pro Ala Ile Leu Ser Ala Ser Pro Gly 1 5 10 15 Glu Lys Val Thr Met Thr Cys Arg Ala Ser Ser Ser Val Ser Tyr Met 20 25 30 His Trp Tyr Gln Gln Lys Pro Gly Ser Ser Pro Lys Pro Trp Ile Tyr 35 40 45 Ala Pro Ser Asn Leu Ala Ser Gly Val Pro Ala Arg Phe Ser Gly Ser 50 55 60 Gly Ser Gly Thr Ser Tyr Ser Leu Thr Ile Ser Arg Val Glu Ala Glu 65 70 75 80 Asp Ala Ala Thr Tyr Tyr Cys Gln Gln Trp Ser Phe Asn Pro Pro Thr 85 90 95 Phe Gly Ala Gly Thr Lys Leu Glu Leu Lys 100 105 <210> 669 <211> 111 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 669 Asp Ile Gln Leu Thr Gln Ser Pro Ser Thr Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Arg Ala Ser Glu Ser Leu Asp Asn Tyr 20 25 30 Gly Ile Arg Phe Leu Thr Trp Phe Gln Gln Lys Pro Gly Lys Ala Pro 35 40 45 Lys Leu Leu Met Tyr Ala Ala Ser Asn Gln Gly Ser Gly Val Pro Ser 50 55 60 Arg Phe Ser Gly Ser Gly Ser Gly Thr Glu Phe Thr Leu Thr Ile Ser 65 70 75 80 Ser Leu Gln Pro Asp Asp Phe Ala Thr Tyr Tyr Cys Gln Gln Thr Lys 85 90 95 Glu Val Pro Trp Ser Phe Gly Gln Gly Thr Lys Val Glu Val Lys 100 105 110 <210> 670 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 670 Glu Ile Val Leu Thr Gln Ser Pro Ala Thr Leu Ser Leu Ser Pro Gly 1 5 10 15 Glu Arg Ala Thr Leu Ser Cys Arg Ala Ser Gln Ser Val Ser Ser Tyr 20 25 30 Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln Ala Pro Arg Leu Leu Ile 35 40 45 Tyr Asp Ala Ser Asn Arg Ala Thr Gly Ile Pro Ala Arg Phe Ser Gly 50 55 60 Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Glu Pro 65 70 75 80 Glu Asp Phe Ala Val Tyr Tyr Cys Gln Gln Arg Ser Asn Trp Pro Pro 85 90 95 Thr Phe Gly Gln Gly Thr Lys Val Glu Ile Lys 100 105 <210> 671 <211> 111 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 671 Asp Ile Val Leu Thr Gln Ser Pro Ala Ser Leu Ala Val Ser Leu Gly 1 5 10 15 Gln Arg Ala Thr Ile Ser Cys Arg Ala Ser Lys Ser Val Ser Thr Ser 20 25 30 Gly Tyr Ser Phe Met His Trp Tyr Gln Gln Lys Pro Gly Gln Pro Pro 35 40 45 Lys Leu Leu Ile Tyr Leu Ala Ser Asn Leu Glu Ser Gly Val Pro Ala 50 55 60 Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Asn Ile His 65 70 75 80 Pro Val Glu Glu Glu Asp Ala Ala Thr Tyr Tyr Cys Gln His Ser Arg 85 90 95 Glu Val Pro Trp Thr Phe Gly Gly Gly Thr Lys Leu Glu Ile Lys 100 105 110 <210> 672 <211> 111 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 672 Asp Ile Val Leu Thr Gln Ser Pro Ala Ser Leu Thr Val Ser Leu Gly 1 5 10 15 Gln Lys Thr Thr Ile Ser Cys Arg Ala Ser Lys Ser Val Ser Thr Ser 20 25 30 Gly Tyr Ser Phe Met His Trp Tyr Gln Leu Lys Pro Gly Gln Ser Pro 35 40 45 Lys Leu Leu Ile Tyr Leu Ala Ser Asp Leu Pro Ser Gly Val Pro Ala 50 55 60 Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Lys Ile His 65 70 75 80 Pro Val Glu Glu Glu Asp Ala Ala Thr Tyr Tyr Cys Gln His Ser Arg 85 90 95 Glu Ile Pro Tyr Thr Phe Gly Gly Gly Thr Lys Leu Glu Ile Thr 100 105 110 <210> 673 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 673 Glu Ile Val Leu Thr Gln Ser Pro Ala Thr Leu Ser Leu Ser Pro Gly 1 5 10 15 Glu Arg Ala Thr Leu Ser Cys Arg Ala Ser Gln Ser Val Ser Ser Tyr 20 25 30 Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln Ala Pro Arg Leu Leu Ile 35 40 45 Tyr Asp Ala Ser Asn Arg Ala Thr Gly Ile Pro Ala Arg Phe Ser Gly 50 55 60 Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Glu Pro 65 70 75 80 Glu Asp Phe Ala Val Tyr Tyr Cys Gln Gln Arg Thr Asn Trp Pro Leu 85 90 95 Thr Phe Gly Gly Gly Thr Lys Val Glu Ile Lys 100 105 <210> 674 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 674 Ala Ile Gln Leu Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Arg Ala Ser Gln Gly Ile Ser Ser Ala 20 25 30 Leu Ala Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Phe Leu Ile 35 40 45 Tyr Asp Ala Ser Ser Leu Glu Ser Gly Val Pro Ser Arg Phe Ser Gly 50 55 60 Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln Pro 65 70 75 80 Glu Asp Phe Ala Thr Tyr Tyr Cys Gln Gln Phe Asn Ser Tyr Pro Phe 85 90 95 Thr Phe Gly Pro Gly Thr Lys Val Asp Ile Lys 100 105 <210> 675 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 675 Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Arg Ala Ser Gln Gly Ile Ser Ser Trp 20 25 30 Leu Ala Trp Tyr Gln Gln Lys Pro Glu Lys Ala Pro Lys Ser Leu Ile 35 40 45 Tyr Ala Ala Ser Ser Leu Gln Ser Gly Val Pro Ser Arg Phe Ser Gly 50 55 60 Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln Pro 65 70 75 80 Glu Asp Phe Ala Thr Tyr Tyr Cys Gln Gln Tyr Asn Ser Tyr Pro Leu 85 90 95 Thr Phe Gly Gly Gly Thr Lys Val Glu Ile Lys 100 105 <210> 676 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 676 Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Arg Ala Ser Gln Gly Ile Ser Ser Trp 20 25 30 Leu Ala Trp Tyr Gln Gln Lys Pro Glu Lys Ala Pro Lys Ser Leu Ile 35 40 45 Tyr Ala Ala Ser Ser Leu Gln Ser Gly Val Pro Ser Arg Phe Ser Gly 50 55 60 Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln Pro 65 70 75 80 Glu Asp Phe Ala Thr Tyr Tyr Cys Gln Gln Tyr Asn Ser Tyr Pro Leu 85 90 95 Thr Phe Gly Gly Gly Thr Lys Val Glu Ile Lys 100 105 <210> 677 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 677 Glu Ile Val Leu Thr Gln Ser Pro Ala Thr Leu Ser Leu Ser Pro Gly 1 5 10 15 Glu Arg Ala Thr Leu Ser Cys Arg Ala Ser Gln Ser Val Ser Ser Tyr 20 25 30 Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln Ala Pro Arg Leu Leu Ile 35 40 45 Phe Asp Ala Ser Asn Arg Ala Thr Gly Ile Pro Ala Arg Phe Ser Gly 50 55 60 Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Glu Pro 65 70 75 80 Glu Asp Phe Ala Val Tyr Tyr Cys Gln Gln Arg Ser Asn Trp Pro Leu 85 90 95 Thr Phe Gly Gly Gly Thr Lys Val Glu Ile Lys 100 105 <210> 678 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 678 Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Val Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Arg Ala Ser Gln Gly Ile Asn Thr Trp 20 25 30 Leu Ala Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile 35 40 45 Tyr Ala Ala Ser Ser Leu Lys Ser Gly Val Pro Ser Arg Phe Ser Gly 50 55 60 Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln Pro 65 70 75 80 Glu Asp Phe Ala Thr Tyr Tyr Cys Gln Gln Ala Asn Ser Phe Pro Leu 85 90 95 Thr Phe Gly Gly Gly Thr Lys Val Glu Ile Lys 100 105 <210> 679 <211> 108 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 679 Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Ser Val Ser Ser Ser Val Ser Ser Ile 20 25 30 Tyr Leu His Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu 35 40 45 Ile Tyr Ser Thr Ser Asn Leu Ala Ser Gly Val Pro Ser Arg Phe Ser 50 55 60 Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln 65 70 75 80 Pro Glu Asp Phe Ala Thr Tyr Tyr Cys Gln Val Tyr Ser Gly Tyr Pro 85 90 95 Leu Thr Phe Gly Gly Gly Thr Lys Val Glu Ile Lys 100 105 <210> 680 <211> 113 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 680 Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Lys Ser Ser Gln Ser Leu Leu Tyr Thr 20 25 30 Ser Ser Gln Lys Asn Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Lys 35 40 45 Ala Pro Lys Leu Leu Ile Tyr Trp Ala Ser Thr Arg Glu Ser Gly Val 50 55 60 Pro Ser Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr 65 70 75 80 Ile Ser Ser Leu Gln Pro Glu Asp Phe Ala Thr Tyr Tyr Cys Gln Gln 85 90 95 Tyr Tyr Ala Tyr Pro Trp Thr Phe Gly Gln Gly Thr Lys Val Glu Ile 100 105 110 Lys <210> 681 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 681 Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Arg Ala Ser Gln Ser Ile Asn Ser Tyr 20 25 30 Leu Asp Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile 35 40 45 Tyr Ala Ala Ser Ser Leu Gln Ser Gly Val Pro Ser Arg Phe Ser Gly 50 55 60 Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln Pro 65 70 75 80 Glu Asp Phe Ala Thr Tyr Tyr Cys Gln Gln Tyr Tyr Ser Thr Pro Phe 85 90 95 Thr Phe Gly Pro Gly Thr Lys Val Glu Ile Lys 100 105 <210> 682 <211> 108 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 682 Glu Ile Val Leu Thr Gln Ser Pro Gly Thr Leu Ser Leu Ser Pro Gly 1 5 10 15 Glu Arg Ala Thr Leu Ser Cys Arg Ala Ser Gln Ser Val Gly Ser Ser 20 25 30 Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln Ala Pro Arg Leu Leu 35 40 45 Ile Tyr Gly Ala Phe Ser Arg Ala Thr Gly Ile Pro Asp Arg Phe Ser 50 55 60 Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Arg Leu Glu 65 70 75 80 Pro Glu Asp Phe Ala Val Tyr Tyr Cys Gln Gln Tyr Gly Ser Ser Pro 85 90 95 Trp Thr Phe Gly Gln Gly Thr Lys Val Glu Ile Lys 100 105 <210> 683 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 683 Glu Ile Val Leu Thr Gln Ser Pro Asp Phe Gln Ser Val Thr Pro Lys 1 5 10 15 Glu Lys Val Thr Ile Thr Cys Arg Ala Ser Gln Ser Ile Gly Ile Ser 20 25 30 Leu His Trp Tyr Gln Gln Lys Pro Asp Gln Ser Pro Lys Leu Leu Ile 35 40 45 Lys Tyr Ala Ser Gln Ser Phe Ser Gly Val Pro Ser Arg Phe Ser Gly 50 55 60 Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Asn Ser Leu Glu Ala 65 70 75 80 Glu Asp Ala Ala Thr Tyr Tyr Cys His Gln Ser Arg Ser Phe Pro Trp 85 90 95 Thr Phe Gly Gln Gly Thr Lys Val Glu Ile Lys 100 105 <210> 684 <211> 113 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 684 Glu Leu Val Met Thr Gln Ser Pro Ser Ser Leu Thr Val Thr Ala Gly 1 5 10 15 Glu Lys Val Thr Met Ser Cys Lys Ser Ser Gln Ser Leu Leu Asn Ser 20 25 30 Gly Asn Gln Lys Asn Tyr Leu Thr Trp Tyr Gln Gln Lys Pro Gly Gln 35 40 45 Pro Pro Lys Leu Leu Ile Tyr Trp Ala Ser Thr Arg Glu Ser Gly Val 50 55 60 Pro Asp Arg Phe Thr Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr 65 70 75 80 Ile Ser Ser Val Gln Ala Glu Asp Leu Ala Val Tyr Tyr Cys Gln Asn 85 90 95 Asp Tyr Ser Tyr Pro Leu Thr Phe Gly Ala Gly Thr Lys Leu Glu Ile 100 105 110 Lys <210> 685 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 685 Glu Leu Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Arg Thr Ser Gln Ser Ile Ser Ser Tyr 20 25 30 Leu Asn Trp Tyr Gln Gln Lys Pro Gly Gln Pro Pro Lys Leu Leu Ile 35 40 45 Tyr Trp Ala Ser Thr Arg Glu Ser Gly Val Pro Asp Arg Phe Ser Gly 50 55 60 Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln Pro 65 70 75 80 Glu Asp Ser Ala Thr Tyr Tyr Cys Gln Gln Ser Tyr Asp Ile Pro Tyr 85 90 95 Thr Phe Gly Gln Gly Thr Lys Leu Glu Ile Lys 100 105 <210> 686 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 686 Asn Ile Val Met Thr Gln Ser Pro Lys Ser Met Ser Met Ser Val Gly 1 5 10 15 Glu Arg Val Thr Leu Thr Cys Lys Ala Ser Glu Asn Val Val Thr Tyr 20 25 30 Val Ser Trp Tyr Gln Gln Lys Pro Glu Gln Ser Pro Lys Leu Leu Ile 35 40 45 Tyr Gly Ala Ser Asn Arg Tyr Thr Gly Val Pro Asp Arg Phe Thr Gly 50 55 60 Ser Gly Ser Ala Thr Asp Phe Thr Leu Thr Ile Ser Ser Val Gln Ala 65 70 75 80 Glu Asp Leu Ala Asp Tyr His Cys Gly Gln Gly Tyr Ser Tyr Pro Tyr 85 90 95 Thr Phe Gly Gly Gly Thr Lys Leu Glu Ile Lys 100 105 <210> 687 <211> 106 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 687 Gln Ile Leu Leu Thr Gln Ser Pro Ala Ile Met Ser Ala Ser Pro Gly 1 5 10 15 Glu Lys Val Thr Met Thr Cys Ser Ala Ser Ser Ser Val Ser Tyr Met 20 25 30 Leu Trp Tyr Gln Gln Lys Pro Gly Ser Ser Pro Lys Pro Trp Ile Phe 35 40 45 Asp Thr Ser Asn Leu Ala Ser Gly Phe Pro Ala Arg Phe Ser Gly Ser 50 55 60 Gly Ser Gly Thr Ser Tyr Ser Leu Ile Ile Ser Ser Met Glu Ala Glu 65 70 75 80 Asp Ala Ala Thr Tyr Tyr Cys His Gln Arg Ser Gly Tyr Pro Tyr Thr 85 90 95 Phe Gly Gly Gly Thr Lys Leu Glu Ile Lys 100 105 <210> 688 <211> 113 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 688 Asp Ile Val Met Thr Gln Ser Pro Asp Ser Leu Ala Val Ser Leu Gly 1 5 10 15 Glu Arg Ala Thr Ile Asn Cys Lys Ser Ser Gln Ser Val Leu Tyr Ser 20 25 30 Ser Asn Asn Lys Asn Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln 35 40 45 Pro Pro Lys Leu Leu Ile Tyr Trp Ala Ser Thr Arg Glu Ser Gly Val 50 55 60 Pro Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr 65 70 75 80 Ile Ser Ser Leu Gln Ala Glu Asp Val Ala Val Tyr Tyr Cys Gln Gln 85 90 95 Tyr Tyr Ser Tyr Pro Leu Thr Phe Gly Gly Gly Thr Lys Val Lys Glu 100 105 110 Ser <210> 689 <211> 112 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 689 Asp Ile Val Met Thr Gln Ser Pro Leu Ser Leu Pro Val Thr Pro Gly 1 5 10 15 Glu Pro Ala Ser Ile Ser Cys Arg Ser Ser Ile Asn Lys Lys Gly Ser 20 25 30 Asn Gly Ile Thr Tyr Leu Tyr Trp Tyr Leu Gln Lys Pro Gly Gln Ser 35 40 45 Pro Gln Leu Leu Ile Tyr Gln Met Ser Asn Leu Ala Ser Gly Val Pro 50 55 60 Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Lys Ile 65 70 75 80 Ser Arg Val Glu Ala Glu Asp Val Gly Val Tyr Tyr Cys Ala Gln Asn 85 90 95 Leu Glu Ile Pro Arg Thr Phe Gly Gln Gly Thr Lys Val Glu Ile Lys 100 105 110 <210> 690 <211> 112 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 690 Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Arg Ser Thr Lys Ser Leu Leu His Ser 20 25 30 Asn Gly Ile Thr Tyr Leu Tyr Trp Tyr Gln Gln Lys Pro Gly Lys Ala 35 40 45 Pro Lys Leu Leu Ile Tyr Gln Met Ser Asn Leu Ala Ser Gly Val Pro 50 55 60 Ser Arg Phe Ser Ser Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile 65 70 75 80 Ser Ser Leu Gln Pro Glu Asp Phe Ala Thr Tyr Tyr Cys Ala Gln Asn 85 90 95 Leu Glu Ile Pro Arg Thr Phe Gly Gln Gly Thr Lys Val Glu Ile Lys 100 105 110 <210> 691 <211> 112 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 691 Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Arg Ser Thr Lys Ser Leu Leu His Ser 20 25 30 Asn Gly Ile Thr Tyr Leu Tyr Trp Tyr Gln Gln Lys Pro Gly Lys Ala 35 40 45 Pro Lys Leu Leu Ile Tyr Gln Met Ser Asn Leu Ala Ser Gly Val Pro 50 55 60 Ser Arg Phe Ser Ser Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile 65 70 75 80 Ser Ser Leu Gln Pro Glu Asp Phe Ala Thr Tyr Tyr Cys Ala Gln Asn 85 90 95 Leu Glu Ile Pro Arg Thr Phe Gly Gln Gly Thr Lys Val Glu Leu Lys 100 105 110 <210> 692 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 692 Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Arg Ala Ser Gln Ser Ile Ser Thr Trp 20 25 30 Leu Ala Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile 35 40 45 Tyr Lys Ala Ser Asn Leu His Thr Gly Val Pro Ser Arg Phe Ser Gly 50 55 60 Ser Gly Ser Gly Thr Glu Phe Ser Leu Thr Ile Ser Gly Leu Gln Pro 65 70 75 80 Asp Asp Phe Ala Thr Tyr Tyr Cys Gln Gln Tyr Asn Ser Tyr Ser Arg 85 90 95 Thr Phe Gly Gln Gly Thr Lys Val Glu Ile Lys 100 105 <210> 693 <211> 110 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 693 Asp Ile Gln Leu Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Ser Val Ser Ser Ser Ile Ser Ser Asn 20 25 30 Asn Leu His Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Pro Trp 35 40 45 Ile Tyr Gly Thr Ser Asn Leu Ala Ser Gly Val Pro Ser Arg Phe Ser 50 55 60 Gly Ser Gly Ser Gly Thr Asp Tyr Thr Phe Thr Ile Ser Ser Leu Gln 65 70 75 80 Pro Glu Asp Ile Ala Thr Tyr Tyr Cys Gln Gln Trp Ser Ser Tyr Pro 85 90 95 Tyr Met Tyr Thr Phe Gly Gln Gly Thr Lys Val Glu Ile Lys 100 105 110 <210> 694 <211> 111 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 694 Asp Ile Val Leu Thr Gln Ser Pro Leu Ser Leu Ala Val Ser Leu Gly 1 5 10 15 Gln Pro Ala Ile Ile Ser Cys Lys Ala Ser Gln Ser Val Ser Phe Ala 20 25 30 Gly Thr Ser Leu Met His Trp Tyr His Gln Lys Pro Gly Gln Gln Pro 35 40 45 Arg Leu Leu Ile Tyr Arg Ala Ser Asn Leu Glu Ala Gly Val Pro Asp 50 55 60 Arg Phe Ser Gly Ser Gly Ser Lys Thr Asp Phe Thr Leu Asn Ile Ser 65 70 75 80 Pro Val Glu Ala Glu Asp Ala Ala Thr Tyr Tyr Cys Gln Gln Ser Arg 85 90 95 Glu Tyr Pro Tyr Thr Phe Gly Gly Gly Thr Lys Leu Glu Ile Lys 100 105 110 <210> 695 <211> 111 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 695 Asp Ile Val Leu Thr Gln Ser Pro Leu Ser Leu Ala Val Ser Leu Gly 1 5 10 15 Gln Pro Ala Ile Ile Ser Cys Lys Ala Ser Gln Ser Val Ser Phe Ala 20 25 30 Gly Thr Ser Leu Met His Trp Tyr His Gln Lys Pro Gly Gln Gln Pro 35 40 45 Arg Leu Leu Ile Tyr Arg Ala Ser Asn Leu Glu Ala Gly Val Pro Asp 50 55 60 Arg Phe Ser Gly Ser Gly Ser Lys Thr Asp Phe Thr Leu Thr Ile Ser 65 70 75 80 Pro Val Glu Ala Glu Asp Ala Ala Thr Tyr Tyr Cys Gln Gln Ser Arg 85 90 95 Glu Tyr Pro Tyr Thr Phe Gly Gly Gly Thr Lys Leu Glu Ile Lys 100 105 110 <210> 696 <211> 100 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 696 Pro Ala Ser Leu Ser Ala Ser Val Gly Glu Thr Val Thr Ile Thr Cys 1 5 10 15 Arg Thr Ser Glu Asn Ile Phe Ser Tyr Leu Ala Trp Tyr Gln Gln Lys 20 25 30 Gln Gly Ile Ser Pro Gln Leu Leu Val Tyr Asn Ala Lys Thr Leu Ala 35 40 45 Glu Gly Val Pro Ser Arg Phe Ser Gly Ser Gly Ser Gly Thr Gln Phe 50 55 60 Ser Leu Lys Ile Asn Ser Leu Gln Pro Glu Asp Phe Gly Ser Tyr Tyr 65 70 75 80 Cys Gln His His Tyr Ala Phe Pro Trp Thr Phe Gly Gly Gly Ser Lys 85 90 95 Leu Glu Ile Lys 100 <210> 697 <211> 112 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 697 Asp Val Val Met Thr Gln Ser Pro Leu Ser Leu Pro Val Thr Pro Gly 1 5 10 15 Glu Pro Ala Ser Ile Ser Cys Arg Ser Ser Gln Ser Leu Val His Ser 20 25 30 Asn Gly Asn Thr Tyr Leu His Trp Tyr Leu Gln Lys Pro Gly Gln Ser 35 40 45 Pro Gln Leu Leu Ile Tyr Lys Val Ser Asn Arg Phe Ser Gly Val Pro 50 55 60 Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Lys Ile 65 70 75 80 Ser Arg Val Glu Ala Glu Asp Val Gly Val Tyr Tyr Cys Ser Gln Asn 85 90 95 Thr His Val Pro Pro Thr Phe Gly Gln Gly Thr Lys Leu Glu Ile Lys 100 105 110 <210> 698 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 698 Glu Ile Val Leu Thr Gln Ser Pro Gly Thr Leu Ser Leu Ser Pro Gly 1 5 10 15 Glu Arg Ala Thr Leu Ser Cys Arg Ala Val Gln Ser Val Ser Ser Ser 20 25 30 Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln Ala Pro Arg Leu Leu 35 40 45 Ile Tyr Gly Ala Ser Ser Arg Ala Thr Gly Ile Pro Asp Arg Phe Ser 50 55 60 Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Arg Leu Glu 65 70 75 80 Pro Glu Asp Phe Ala Val Tyr Tyr Cys Gln Gln Tyr Gly Ser Ser Pro 85 90 95 Thr Phe Gly Gly Gly Thr Lys Val Glu Ile Lys 100 105 <210> 699 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 699 Glu Ile Val Leu Thr Gln Ser Pro Gly Thr Leu Ser Leu Ser Pro Gly 1 5 10 15 Glu Arg Ala Thr Leu Ser Cys Arg Ala Ser Gln Ser Val Ser Ser Ser 20 25 30 Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln Ala Pro Arg Leu Leu 35 40 45 Ile Tyr Gly Ala Ser Ser Arg Ala Thr Gly Ile Pro Asp Arg Phe Ser 50 55 60 Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Arg Leu Glu 65 70 75 80 Pro Glu Asp Phe Ala Val Tyr Tyr Cys Gln Gln Tyr Gly Ser Ser Pro 85 90 95 Thr Phe Gly Gly Gly Thr Lys Val Glu Ile Lys 100 105 <210> 700 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 700 Glu Ile Leu Leu Thr Gln Ser Pro Gly Thr Leu Ser Leu Ser Pro Gly 1 5 10 15 Glu Arg Ala Thr Leu Ser Cys Arg Ala Ser Gln Ser Val Ser Ser Ser 20 25 30 Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln Ala Pro Arg Leu Leu 35 40 45 Ile Tyr Gly Ala Ser Ser Arg Ala Thr Gly Ile Pro Asp Arg Phe Ser 50 55 60 Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Arg Leu Glu 65 70 75 80 Pro Glu Asp Phe Ala Val Tyr Tyr Cys Gln Gln Tyr Gly Ser Ser Pro 85 90 95 Thr Phe Gly Gln Gly Thr Lys Val Glu Ile Lys 100 105 <210> 701 <211> 112 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 701 Asp Thr Val Met Thr Gln Thr Pro Leu Ser Ser His Val Thr Leu Gly 1 5 10 15 Gln Pro Ala Ser Ile Ser Cys Arg Ser Ser Gln Ser Leu Val His Ser 20 25 30 Asp Gly Asn Thr Tyr Leu Ser Trp Leu Gln Gln Arg Pro Gly Gln Pro 35 40 45 Pro Arg Leu Leu Ile Tyr Arg Ile Ser Arg Arg Phe Ser Gly Val Pro 50 55 60 Asp Arg Phe Ser Gly Ser Gly Ala Gly Thr Asp Phe Thr Leu Glu Ile 65 70 75 80 Ser Arg Val Glu Ala Glu Asp Val Gly Val Tyr Tyr Cys Met Gln Ser 85 90 95 Thr His Val Pro Arg Thr Phe Gly Gln Gly Thr Lys Val Glu Ile Lys 100 105 110 <210> 702 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 702 Asp Ile Leu Leu Thr Gln Ser Pro Val Ile Leu Ser Val Ser Pro Gly 1 5 10 15 Glu Arg Val Ser Phe Ser Cys Arg Ala Ser Gln Ser Ile Gly Thr Asn 20 25 30 Ile His Trp Tyr Gln Gln Arg Thr Asn Gly Ser Pro Arg Leu Leu Ile 35 40 45 Lys Tyr Ala Ser Glu Ser Ile Ser Gly Ile Pro Ser Arg Phe Ser Gly 50 55 60 Ser Gly Ser Gly Thr Asp Phe Thr Leu Ser Ile Asn Ser Val Glu Ser 65 70 75 80 Glu Asp Ile Ala Asp Tyr Tyr Cys Gln Gln Asn Asn Asn Trp Pro Thr 85 90 95 Thr Phe Gly Ala Gly Thr Lys Leu Glu Leu Lys 100 105 <210> 703 <211> 106 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 703 Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Arg Ala Ser Gln Gly Ile Asn Asn Tyr 20 25 30 Leu Asn Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Arg Leu Ile 35 40 45 Tyr Asn Thr Asn Asn Leu Gln Thr Gly Val Pro Ser Arg Phe Ser Gly 50 55 60 Ser Gly Ser Gly Thr Glu Phe Thr Leu Thr Ile Ser Ser Leu Gln Pro 65 70 75 80 Glu Asp Phe Ala Thr Tyr Tyr Cys Leu Gln His Asn Ser Phe Pro Thr 85 90 95 Phe Gly Gln Gly Thr Lys Leu Glu Ile Lys 100 105 <210> 704 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 704 Ala Ile Gln Leu Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Arg Ala Ser Gln Asp Ile Ser Ser Ala 20 25 30 Leu Val Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile 35 40 45 Tyr Asp Ala Ser Ser Leu Glu Ser Gly Val Pro Ser Arg Phe Ser Gly 50 55 60 Ser Glu Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln Pro 65 70 75 80 Glu Asp Phe Ala Thr Tyr Tyr Cys Gln Gln Phe Asn Ser Tyr Pro Leu 85 90 95 Thr Phe Gly Gly Gly Thr Lys Val Glu Ile Lys 100 105 <210> 705 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 705 Glu Ile Val Met Thr Gln Ser Pro Ala Thr Leu Ser Leu Ser Pro Gly 1 5 10 15 Glu Arg Ala Thr Leu Ser Cys Arg Ala Ser Gln Ser Val Ser Ser Tyr 20 25 30 Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln Ala Pro Arg Leu Leu Ile 35 40 45 Tyr Asp Ala Ser Asn Arg Ala Thr Gly Ile Pro Ala Arg Phe Ser Gly 50 55 60 Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Glu Pro 65 70 75 80 Glu Asp Phe Ala Val Tyr Tyr Cys His Gln Tyr Gly Ser Thr Pro Leu 85 90 95 Thr Phe Gly Gly Gly Thr Lys Ala Glu Ile Lys 100 105 <210> 706 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 706 Asp Ile Gln Met Thr Gln Ser Pro Ser Thr Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Arg Ala Ser Gln Ser Ile Ser Ser Trp 20 25 30 Trp Ala Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile 35 40 45 Tyr Asp Ala Ser Ser Leu Glu Ser Gly Val Pro Ser Arg Phe Ser Gly 50 55 60 Ser Gly Ser Gly Thr Glu Phe Thr Leu Thr Ile Ser Ser Leu Gln Pro 65 70 75 80 Asp Asp Phe Ala Thr Tyr Tyr Cys Gln Gln Tyr His Ala His Pro Thr 85 90 95 Thr Phe Gly Gly Gly Thr Lys Val Glu Ile Lys 100 105 <210> 707 <211> 113 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 707 Asp Ile Val Met Thr Gln Ser Pro Asp Ser Leu Ala Val Ser Leu Gly 1 5 10 15 Glu Arg Ala Thr Ile Asn Cys Lys Ser Ser Gln Ser Val Leu Tyr Ser 20 25 30 Pro Asn Asn Lys Asn Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln 35 40 45 Pro Pro Lys Leu Leu Ile Tyr Trp Ala Ser Thr Arg Glu Ser Gly Val 50 55 60 Pro Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr 65 70 75 80 Ile Ser Ser Leu Gln Ala Glu Asp Val Ala Val Tyr Tyr Cys Gln Gln 85 90 95 Tyr Tyr Gly Ser Pro Ile Thr Phe Gly Gly Gly Thr Lys Val Glu Ile 100 105 110 Lys <210> 708 <211> 108 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 708 Glu Ile Val Met Thr Gln Ser Pro Ala Thr Leu Ser Val Ser Pro Gly 1 5 10 15 Glu Arg Ala Thr Leu Ser Cys Arg Ala Ser Gln Ser Val Ser Ser Asn 20 25 30 Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln Ala Pro Arg Leu Leu Ile 35 40 45 Tyr Gly Ala Ser Thr Arg Ala Thr Gly Ile Pro Ala Arg Phe Ser Gly 50 55 60 Ser Gly Ser Gly Thr Glu Phe Thr Leu Thr Ile Ser Ser Leu Gln Ser 65 70 75 80 Glu Asp Phe Ala Val Tyr Tyr Cys Gln Asp Tyr Arg Thr Trp Pro Arg 85 90 95 Arg Val Phe Gly Gly Gly Thr Lys Val Glu Ile Lys 100 105 <210> 709 <211> 112 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 709 Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Arg Ser Ser Gln Asn Ile Val His Ser 20 25 30 Asn Gly Asn Thr Tyr Leu Asp Trp Tyr Gln Gln Thr Pro Gly Lys Ala 35 40 45 Pro Lys Leu Leu Ile Tyr Lys Val Ser Asn Arg Phe Ser Gly Val Pro 50 55 60 Ser Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Phe Thr Ile 65 70 75 80 Ser Ser Leu Gln Pro Glu Asp Ile Ala Thr Tyr Tyr Cys Phe Gln Tyr 85 90 95 Ser His Val Pro Trp Thr Phe Gly Gln Gly Thr Lys Leu Gln Ile Thr 100 105 110 <210> 710 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 710 Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Gln Ala Ser Gln Asp Ile Ser Asn Tyr 20 25 30 Leu Asn Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile 35 40 45 Tyr Asp Ala Ser Asn Leu Glu Thr Gly Val Pro Ser Arg Phe Ser Gly 50 55 60 Ser Gly Ser Gly Thr Asp Phe Thr Phe Thr Ile Ser Ser Leu Gln Pro 65 70 75 80 Glu Asp Ile Ala Thr Tyr Phe Cys Gln His Phe Asp His Leu Pro Leu 85 90 95 Ala Phe Gly Gly Gly Thr Lys Val Glu Ile Lys 100 105 <210> 711 <211> 112 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 711 Asp Val Val Met Thr Gln Thr Pro Leu Ser Leu Pro Val Ser Leu Gly 1 5 10 15 Asp Gln Ala Ser Ile Ser Cys Arg Ser Ser Gln Ser Leu Val His Ser 20 25 30 Asn Gly Asn Thr Tyr Leu His Trp Tyr Leu Gln Lys Pro Gly Gln Ser 35 40 45 Pro Lys Leu Leu Ile Tyr Lys Val Ser Asn Arg Phe Ser Gly Val Pro 50 55 60 Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Lys Ile 65 70 75 80 Ser Arg Val Glu Ala Glu Asp Leu Gly Val Tyr Phe Cys Ser Gln Ser 85 90 95 Thr His Val Pro Trp Thr Phe Gly Gly Gly Thr Lys Leu Glu Ile Lys 100 105 110 <210> 712 <211> 111 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 712 Asp Val Val Met Thr Gln Thr Pro Leu Ser Leu Pro Val Ser Leu Gly 1 5 10 15 Asp Gln Ala Ser Ile Ser Cys Arg Ser Ser Gln Ser Leu Val His Ser 20 25 30 Asn Gly Asn Thr Tyr Leu His Trp Tyr Leu Gln Lys Pro Gly Gln Ser 35 40 45 Pro Lys Leu Leu Ile Tyr Lys Val Ser Asn Arg Phe Ser Gly Val Pro 50 55 60 Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Lys Ile 65 70 75 80 Ser Arg Val Glu Ala Glu Asp Leu Gly Val Tyr Phe Cys Ser Gln Ser 85 90 95 Thr His Val Leu Thr Phe Gly Ser Gly Thr Lys Leu Glu Ile Lys 100 105 110 <210> 713 <211> 102 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 713 Gln Ser Pro Ser Phe Leu Ser Ala Phe Val Gly Asp Arg Ile Thr Ile 1 5 10 15 Thr Cys Arg Ala Ser Pro Gly Ile Arg Asn Tyr Leu Ala Trp Tyr Gln 20 25 30 Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile Tyr Ala Ala Ser Thr 35 40 45 Leu Gln Ser Gly Val Pro Ser Arg Phe Ser Gly Ser Gly Ser Gly Thr 50 55 60 Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln Pro Glu Asp Phe Ala Thr 65 70 75 80 Tyr Tyr Cys Gln Gln Tyr Asn Ser Tyr Pro Leu Ser Phe Gly Gly Gly 85 90 95 Thr Lys Val Glu Ile Lys 100 <210> 714 <211> 110 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 714 Gln Ala Val Val Thr Gln Glu Pro Ser Phe Ser Val Ser Pro Gly Gly 1 5 10 15 Thr Val Thr Leu Thr Cys Gly Leu Ser Ser Gly Ser Val Ser Thr Ser 20 25 30 Tyr Tyr Pro Ser Trp Tyr Gln Gln Thr Pro Gly Gln Ala Pro Arg Thr 35 40 45 Leu Ile Tyr Ser Thr Asn Thr Arg Ser Ser Gly Val Pro Asp Arg Phe 50 55 60 Ser Gly Ser Ile Leu Gly Asn Lys Ala Ala Leu Thr Ile Thr Gly Ala 65 70 75 80 Gln Ala Asp Asp Glu Ser Asp Tyr Tyr Cys Val Leu Tyr Met Gly Ser 85 90 95 Gly Gln Tyr Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 100 105 110 <210> 715 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 715 Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Arg Ala Ser Gln Asp Val Asn Thr Ala 20 25 30 Val Ala Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile 35 40 45 Tyr Ser Ala Ser Phe Leu Tyr Ser Gly Val Pro Ser Arg Phe Ser Gly 50 55 60 Ser Arg Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln Pro 65 70 75 80 Glu Asp Phe Ala Thr Tyr Tyr Cys Gln Gln His Tyr Thr Thr Pro Pro 85 90 95 Thr Phe Gly Gln Gly Thr Lys Val Glu Ile Lys 100 105 <210> 716 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 716 Asp Ile Val Met Thr Gln Ser His Lys Phe Met Ser Thr Ser Val Gly 1 5 10 15 Asp Arg Val Ser Ile Thr Cys Lys Ala Ser Gln Asp Val Asn Thr Ala 20 25 30 Val Ala Trp Tyr Gln Gln Lys Pro Gly His Ser Pro Lys Leu Leu Ile 35 40 45 Tyr Ser Ala Ser Phe Arg Tyr Thr Gly Val Pro Asp Arg Phe Thr Gly 50 55 60 Ser Arg Ser Gly Thr Asp Phe Thr Phe Thr Ile Ser Ser Val Gln Ala 65 70 75 80 Glu Asp Leu Ala Val Tyr Tyr Cys Gln Gln His Tyr Thr Thr Pro Pro 85 90 95 Thr Phe Gly Gly Gly Thr Lys Val Glu Ile Lys 100 105 <210> 717 <211> 111 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 717 Gln Ser Val Leu Thr Gln Pro Pro Ser Val Ser Gly Ala Pro Gly Gln 1 5 10 15 Arg Val Thr Ile Ser Cys Thr Gly Ser Ser Ser Asn Ile Gly Ala Gly 20 25 30 Tyr Gly Val His Trp Tyr Gln Gln Leu Pro Gly Thr Ala Pro Lys Leu 35 40 45 Leu Ile Tyr Gly Asn Thr Asn Arg Pro Ser Gly Val Pro Asp Arg Phe 50 55 60 Ser Gly Phe Lys Ser Gly Thr Ser Ala Ser Leu Ala Ile Thr Gly Leu 65 70 75 80 Gln Ala Glu Asp Glu Ala Asp Tyr Tyr Cys Gln Phe Tyr Asp Ser Ser 85 90 95 Leu Ser Gly Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 100 105 110 <210> 718 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 718 Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Lys Ala Ser Gln Asp Val Ser Ile Gly 20 25 30 Val Ala Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile 35 40 45 Tyr Ser Ala Ser Tyr Arg Tyr Thr Gly Val Pro Ser Arg Phe Ser Gly 50 55 60 Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln Pro 65 70 75 80 Glu Asp Phe Ala Thr Tyr Tyr Cys Gln Gln Tyr Tyr Ile Tyr Pro Tyr 85 90 95 Thr Phe Gly Gln Gly Thr Lys Val Glu Ile Lys 100 105 <210> 719 <211> 111 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 719 Gln Ser Ala Leu Thr Gln Pro Ala Ser Val Ser Gly Ser Pro Gly Gln 1 5 10 15 Ser Ile Thr Ile Ser Cys Thr Gly Thr Ser Ser Asp Val Gly Ser Tyr 20 25 30 Asn Val Val Ser Trp Tyr Gln Gln His Pro Gly Lys Ala Pro Lys Leu 35 40 45 Ile Ile Tyr Glu Val Ser Gln Arg Pro Ser Gly Val Ser Asn Arg Phe 50 55 60 Ser Gly Ser Lys Ser Gly Asn Thr Ala Ser Leu Thr Ile Ser Gly Leu 65 70 75 80 Gln Thr Glu Asp Glu Ala Asp Tyr Tyr Cys Cys Ser Tyr Ala Gly Ser 85 90 95 Ser Ile Phe Val Ile Phe Gly Gly Gly Thr Lys Val Thr Val Leu 100 105 110 <210> 720 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 720 Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Arg Ala Ser Gln Asn Ile Ala Thr Asp 20 25 30 Val Ala Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile 35 40 45 Tyr Ser Ala Ser Phe Leu Tyr Ser Gly Val Pro Ser Arg Phe Ser Gly 50 55 60 Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln Pro 65 70 75 80 Glu Asp Phe Ala Thr Tyr Tyr Cys Gln Gln Ser Glu Pro Glu Pro Tyr 85 90 95 Thr Phe Gly Gln Gly Thr Lys Val Glu Ile Lys 100 105 <210> 721 <211> 111 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 721 Gln Ser Ala Leu Thr Gln Pro Ala Ser Val Ser Gly Ser Pro Gly Gln 1 5 10 15 Ser Ile Thr Ile Ser Cys Thr Gly Thr Ser Ser Asp Val Gly Gly Tyr 20 25 30 Asn Phe Val Ser Trp Tyr Gln Gln His Pro Gly Lys Ala Pro Lys Leu 35 40 45 Met Ile Tyr Asp Val Ser Asp Arg Pro Ser Gly Val Ser Asp Arg Phe 50 55 60 Ser Gly Ser Lys Ser Gly Asn Thr Ala Ser Leu Ile Ile Ser Gly Leu 65 70 75 80 Gln Ala Asp Asp Glu Ala Asp Tyr Tyr Cys Ser Ser Tyr Gly Ser Ser 85 90 95 Ser Thr His Val Ile Phe Gly Gly Gly Thr Lys Val Thr Val Leu 100 105 110 <210> 722 <211> 110 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 722 Gln Ser Val Leu Thr Gln Pro Pro Ser Val Ser Ala Ala Pro Gly Gln 1 5 10 15 Lys Val Thr Ile Ser Cys Ser Gly Ser Ser Ser Asn Ile Gly Asn Asn 20 25 30 Tyr Val Ser Trp Tyr Gln Gln Leu Pro Gly Thr Ala Pro Lys Leu Leu 35 40 45 Ile Tyr Asp His Thr Asn Arg Pro Ala Gly Val Pro Asp Arg Phe Ser 50 55 60 Gly Ser Lys Ser Gly Thr Ser Ala Ser Leu Ala Ile Ser Gly Phe Arg 65 70 75 80 Ser Glu Asp Glu Ala Asp Tyr Tyr Cys Ala Ser Trp Asp Tyr Thr Leu 85 90 95 Ser Gly Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 100 105 110 <210> 723 <211> 112 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 723 Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Arg Ser Ser Gln Arg Ile Val His Ser 20 25 30 Asn Gly Asn Thr Tyr Leu Glu Trp Tyr Gln Gln Thr Pro Gly Lys Ala 35 40 45 Pro Lys Leu Leu Ile Tyr Lys Val Ser Asn Arg Phe Ser Gly Val Pro 50 55 60 Ser Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Phe Thr Ile 65 70 75 80 Ser Ser Leu Gln Pro Glu Asp Ile Ala Thr Tyr Tyr Cys Phe Gln Gly 85 90 95 Ser His Val Pro Phe Thr Phe Gly Gln Gly Thr Lys Leu Gln Ile Thr 100 105 110 <210> 724 <211> 111 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 724 Asp Ile Ala Leu Thr Gln Pro Ala Ser Val Ser Gly Ser Pro Gly Gln 1 5 10 15 Ser Ile Thr Ile Ser Cys Thr Gly Thr Ser Ser Asp Ile Gly Gly Tyr 20 25 30 Asn Ser Val Ser Trp Tyr Gln Gln His Pro Gly Lys Ala Pro Lys Leu 35 40 45 Met Ile Tyr Gly Val Asn Asn Arg Pro Ser Gly Val Ser Asn Arg Phe 50 55 60 Ser Gly Ser Lys Ser Gly Asn Thr Ala Ser Leu Thr Ile Ser Gly Leu 65 70 75 80 Gln Ala Glu Asp Glu Ala Asp Tyr Tyr Cys Ser Ser Tyr Asp Ile Glu 85 90 95 Ser Ala Thr Pro Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu 100 105 110 <210> 725 <211> 106 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 725 Asp Ile Glu Leu Thr Gln Ser Pro Ala Ile Met Ser Ala Ser Pro Gly 1 5 10 15 Glu Lys Val Thr Met Thr Cys Ser Ala Ser Ser Ser Val Ser Tyr Met 20 25 30 His Trp Tyr Gln Gln Lys Ser Gly Thr Ser Pro Lys Arg Trp Ile Tyr 35 40 45 Asp Thr Ser Lys Leu Ala Ser Gly Val Pro Gly Arg Phe Ser Gly Ser 50 55 60 Gly Ser Gly Asn Ser Tyr Ser Leu Thr Ile Ser Ser Val Glu Ala Glu 65 70 75 80 Asp Asp Ala Thr Tyr Tyr Cys Gln Gln Trp Ser Gly Tyr Pro Leu Thr 85 90 95 Phe Gly Ala Gly Thr Lys Leu Glu Ile Lys 100 105 <210> 726 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 726 Glu Ile Val Leu Thr Gln Ser Pro Ala Thr Leu Ser Leu Ser Pro Gly 1 5 10 15 Glu Arg Ala Thr Leu Ser Cys Arg Ala Ser Gln Ser Val Ser Ser Tyr 20 25 30 Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln Ala Pro Arg Leu Leu Ile 35 40 45 Tyr Asp Ala Ser Asn Arg Ala Thr Gly Ile Pro Ala Arg Phe Ser Gly 50 55 60 Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Glu Pro 65 70 75 80 Glu Asp Phe Ala Val Tyr Tyr Cys Gln Gln Arg Ser Asn Trp Pro Leu 85 90 95 Thr Phe Gly Gly Gly Thr Lys Val Glu Ile Lys 100 105 <210> 727 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 727 Glu Ile Val Leu Thr Gln Ser Pro Ala Thr Leu Ser Leu Ser Pro Gly 1 5 10 15 Glu Arg Ala Thr Leu Ser Cys Arg Ala Ser Gln Ser Val Ser Ser Tyr 20 25 30 Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln Ala Pro Arg Leu Leu Ile 35 40 45 Tyr Asp Ala Ser Asn Arg Ala Thr Gly Ile Pro Ala Arg Phe Ser Gly 50 55 60 Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Glu Pro 65 70 75 80 Glu Asp Phe Ala Val Tyr Tyr Cys Gln Gln Arg Ser Asn Trp Pro Leu 85 90 95 Thr Phe Gly Gly Gly Thr Lys Val Glu Ile Lys 100 105 <210> 728 <211> 108 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 728 Glu Ile Val Leu Thr Gln Ser Pro Gly Thr Leu Ser Leu Ser Pro Gly 1 5 10 15 Glu Arg Ala Thr Leu Ser Cys Arg Ala Ser Gln Ser Val Ser Ser Ser 20 25 30 Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln Ala Pro Arg Leu Leu 35 40 45 Ile Tyr Gly Ala Ser Ser Arg Ala Thr Gly Ile Pro Asp Arg Phe Ser 50 55 60 Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Arg Leu Glu 65 70 75 80 Pro Glu Asp Phe Ala Val Tyr Tyr Cys Gln Gln Tyr Gly Ser Ser Gln 85 90 95 Tyr Thr Phe Gly Gln Gly Thr Lys Leu Glu Ile Lys 100 105 <210> 729 <211> 106 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 729 Asp Ile Glu Leu Thr Gln Ser Pro Ala Ile Met Ser Ala Ser Pro Gly 1 5 10 15 Glu Lys Val Thr Met Thr Cys Ser Ala Ser Ser Ser Val Ser Tyr Met 20 25 30 His Trp Tyr Gln Gln Lys Ser Gly Thr Ser Pro Lys Arg Trp Ile Tyr 35 40 45 Asp Thr Ser Lys Leu Ala Ser Gly Val Pro Gly Arg Phe Ser Gly Ser 50 55 60 Gly Ser Gly Asn Ser Tyr Ser Leu Thr Ile Ser Ser Val Glu Ala Glu 65 70 75 80 Asp Asp Ala Thr Tyr Tyr Cys Gln Gln Trp Ser Lys His Pro Leu Thr 85 90 95 Phe Gly Ser Gly Thr Lys Val Glu Ile Lys 100 105 <210> 730 <211> 108 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 730 Asp Ile Val Met Thr Gln Ser Pro Ala Ile Met Ser Ala Ser Pro Gly 1 5 10 15 Glu Lys Val Thr Met Thr Cys Ser Ala Ser Ser Ser Val Ser Ser Ser 20 25 30 Tyr Leu Tyr Trp Tyr Gln Gln Lys Pro Gly Ser Ser Pro Lys Leu Trp 35 40 45 Ile Tyr Ser Thr Ser Asn Leu Ala Ser Gly Val Pro Ala Arg Phe Ser 50 55 60 Gly Ser Gly Ser Gly Thr Ser Tyr Ser Leu Thr Ile Ser Ser Met Glu 65 70 75 80 Ala Glu Asp Ala Ala Ser Tyr Phe Cys His Gln Trp Asn Arg Tyr Pro 85 90 95 Tyr Thr Phe Gly Gly Gly Thr Lys Leu Glu Ile Lys 100 105 <210> 731 <211> 108 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 731 Asp Ile Gln Leu Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Met Thr Cys Ser Ala Ser Ser Ser Val Ser Ser Ser 20 25 30 Tyr Leu Tyr Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Trp 35 40 45 Ile Tyr Ser Thr Ser Asn Leu Ala Ser Gly Val Pro Ala Arg Phe Ser 50 55 60 Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln 65 70 75 80 Pro Glu Asp Ser Ala Ser Tyr Phe Cys His Gln Trp Asn Arg Tyr Pro 85 90 95 Tyr Thr Phe Gly Gly Gly Thr Arg Leu Glu Ile Lys 100 105 <210> 732 <211> 106 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 732 Glu Ile Val Leu Thr Gln Ser Pro Ala Thr Met Ser Ala Ser Pro Gly 1 5 10 15 Glu Arg Val Thr Ile Thr Cys Ser Ala His Ser Ser Val Ser Phe Met 20 25 30 His Trp Phe Gln Gln Lys Pro Gly Thr Ser Pro Lys Leu Trp Ile Tyr 35 40 45 Ser Thr Ser Ser Leu Ala Ser Gly Val Pro Ala Arg Phe Gly Gly Ser 50 55 60 Gly Ser Gly Thr Ser Tyr Ser Leu Thr Ile Ser Ser Met Glu Ala Glu 65 70 75 80 Asp Ala Ala Thr Tyr Tyr Cys Gln Gln Arg Ser Ser Phe Pro Leu Thr 85 90 95 Phe Gly Ala Gly Thr Lys Leu Glu Leu Lys 100 105 <210> 733 <211> 113 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 733 Asp Ile Val Met Ser Gln Ser Pro Ser Ser Leu Ala Val Ser Val Gly 1 5 10 15 Glu Lys Val Thr Met Ser Cys Lys Ser Ser Gln Ser Leu Leu Tyr Ser 20 25 30 Ser Asn Gln Lys Ile Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln 35 40 45 Ser Pro Lys Leu Leu Ile Tyr Trp Ala Ser Thr Arg Glu Ser Gly Val 50 55 60 Pro Asp Arg Phe Thr Gly Gly Gly Ser Gly Thr Asp Phe Thr Leu Thr 65 70 75 80 Ile Ser Ser Val Lys Ala Glu Asp Leu Ala Val Tyr Tyr Cys Gln Gln 85 90 95 Tyr Tyr Arg Tyr Pro Arg Thr Phe Gly Gly Gly Thr Lys Leu Glu Ile 100 105 110 Lys <210> 734 <211> 113 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 734 Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Lys Ser Ser Gln Ser Leu Leu Tyr Ser 20 25 30 Ser Asn Gln Lys Ile Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Lys 35 40 45 Ala Pro Lys Leu Leu Ile Tyr Trp Ala Ser Thr Arg Glu Ser Gly Val 50 55 60 Pro Ser Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Phe Thr 65 70 75 80 Ile Ser Ser Leu Gln Pro Glu Asp Ile Ala Thr Tyr Tyr Cys Gln Gln 85 90 95 Tyr Tyr Arg Tyr Pro Arg Thr Phe Gly Gln Gly Thr Lys Val Glu Ile 100 105 110 Lys <210> 735 <211> 106 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 735 Glu Ile Val Leu Thr Gln Ser Pro Ala Thr Leu Ser Leu Ser Pro Gly 1 5 10 15 Glu Arg Ala Thr Leu Ser Cys Arg Ala Ser Gln Ser Val Ser Ser Tyr 20 25 30 Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln Ala Pro Arg Leu Leu Ile 35 40 45 Tyr Asp Ala Ser Asn Arg Ala Thr Gly Ile Pro Ala Arg Phe Ser Gly 50 55 60 Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Glu Pro 65 70 75 80 Glu Asp Phe Ala Val Tyr Tyr Cys Gln Gln Arg Ser Asn Trp Pro Thr 85 90 95 Phe Gly Gln Gly Thr Lys Val Glu Ile Lys 100 105 <210> 736 <211> 108 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 736 Glu Ile Val Leu Thr Gln Ser Pro Gly Thr Leu Ser Leu Ser Pro Gly 1 5 10 15 Glu Arg Ala Thr Leu Ser Cys Arg Ala Ser Gln Arg Val Ser Ser Ser 20 25 30 Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln Ala Pro Arg Leu Leu 35 40 45 Ile Tyr Asp Ala Ser Ser Arg Ala Thr Gly Ile Pro Asp Arg Phe Ser 50 55 60 Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Arg Leu Glu 65 70 75 80 Pro Glu Asp Phe Ala Val Tyr Tyr Cys Gln Gln Tyr Gly Ser Leu Pro 85 90 95 Trp Thr Phe Gly Gln Gly Thr Lys Val Glu Ile Lys 100 105 <210> 737 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 737 Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Arg Ala Ser Gln Asp Val Ser Thr Ala 20 25 30 Val Ala Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile 35 40 45 Tyr Ser Ala Ser Phe Leu Tyr Ser Gly Val Pro Ser Arg Phe Ser Gly 50 55 60 Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln Pro 65 70 75 80 Glu Asp Phe Ala Thr Tyr Tyr Cys Gln Gln Tyr Leu Tyr His Pro Ala 85 90 95 Thr Phe Gly Gln Gly Thr Lys Val Glu Ile Lys 100 105 <210> 738 <211> 110 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 738 Gln Ser Ala Leu Thr Gln Pro Ala Ser Val Ser Gly Ser Pro Gly Gln 1 5 10 15 Ser Ile Thr Ile Ser Cys Thr Gly Thr Ser Ser Asp Val Gly Gly Tyr 20 25 30 Asn Tyr Val Ser Trp Tyr Gln Gln His Pro Gly Lys Ala Pro Lys Leu 35 40 45 Met Ile Tyr Asp Val Ser Asn Arg Pro Ser Gly Val Ser Asn Arg Phe 50 55 60 Ser Gly Ser Lys Ser Gly Asn Thr Ala Ser Leu Thr Ile Ser Gly Leu 65 70 75 80 Gln Ala Glu Asp Glu Ala Asp Tyr Tyr Cys Ser Ser Tyr Thr Ser Ser 85 90 95 Ser Thr Arg Val Phe Gly Thr Gly Thr Lys Val Thr Val Leu 100 105 110 <210> 739 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 739 Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Thr Ser Val Gly 1 5 10 15 Asp Arg Val Thr Leu Thr Cys Lys Ala Ser Gln Asp Val Gly Thr Ala 20 25 30 Val Asp Trp Tyr Gln Gln Lys Pro Gly Pro Ser Pro Lys Leu Leu Ile 35 40 45 Tyr Trp Ala Ser Thr Arg His Thr Gly Ile Pro Ser Arg Phe Ser Gly 50 55 60 Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln Pro 65 70 75 80 Glu Asp Phe Ala Asp Tyr Tyr Cys Gln Gln Tyr Asn Ser Tyr Pro Leu 85 90 95 Thr Phe Gly Pro Gly Thr Lys Val Asp Ile Lys 100 105 <210> 740 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 740 Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Lys Ala Ser Gln Asn Val Asp Thr Asn 20 25 30 Val Ala Trp Tyr Gln Gln Lys Pro Gly Gln Ala Pro Lys Ser Leu Ile 35 40 45 Tyr Ser Ala Ser Tyr Arg Tyr Ser Asp Val Pro Ser Arg Phe Ser Gly 50 55 60 Ser Ala Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Val Gln Ser 65 70 75 80 Glu Asp Phe Ala Thr Tyr Tyr Cys Gln Gln Tyr Asp Ser Tyr Pro Tyr 85 90 95 Thr Phe Gly Gly Gly Thr Lys Leu Glu Ile Lys 100 105 <210> 741 <211> 112 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 741 Glu Leu Val Leu Thr Gln Ser Pro Ser Val Ser Ala Ala Leu Gly Ser 1 5 10 15 Pro Ala Lys Ile Thr Cys Thr Leu Ser Ser Ala His Lys Thr Asp Thr 20 25 30 Ile Asp Trp Tyr Gln Gln Leu Gln Gly Glu Ala Pro Arg Tyr Leu Met 35 40 45 Gln Val Gln Ser Asp Gly Ser Tyr Thr Lys Arg Pro Gly Val Pro Asp 50 55 60 Arg Phe Ser Gly Ser Ser Ser Gly Ala Asp Arg Tyr Leu Ile Ile Pro 65 70 75 80 Ser Val Gln Ala Asp Asp Glu Ala Asp Tyr Tyr Cys Gly Ala Asp Tyr 85 90 95 Ile Gly Gly Tyr Val Phe Gly Gly Gly Thr Gln Leu Thr Val Thr Gly 100 105 110 <210> 742 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 742 Asp Ile Lys Met Thr Gln Ser Pro Ser Ser Met Tyr Ala Ser Leu Gly 1 5 10 15 Glu Arg Val Thr Ile Thr Cys Lys Ala Ser Pro Asp Ile Asn Ser Tyr 20 25 30 Leu Ser Trp Phe Gln Gln Lys Pro Gly Lys Ser Pro Lys Thr Leu Ile 35 40 45 Tyr Arg Ala Asn Arg Leu Val Asp Gly Val Pro Ser Arg Phe Ser Gly 50 55 60 Gly Gly Ser Gly Gln Asp Tyr Ser Leu Thr Ile Asn Ser Leu Glu Tyr 65 70 75 80 Glu Asp Met Gly Ile Tyr Tyr Cys Leu Gln Tyr Asp Glu Phe Pro Tyr 85 90 95 Thr Phe Gly Gly Gly Thr Lys Leu Glu Met Lys 100 105 <210> 743 <211> 108 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 743 Glu Leu Val Met Thr Gln Thr Pro Ser Ser Val Ser Ala Ala Val Gly 1 5 10 15 Gly Thr Val Thr Ile Asn Cys Gln Ala Ser Gln Ser Ile Gly Ser Tyr 20 25 30 Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln Pro Pro Lys Leu Leu Ile 35 40 45 Tyr Tyr Ala Ser Asn Leu Ala Ser Gly Val Pro Ser Arg Phe Ser Gly 50 55 60 Ser Gly Ser Gly Thr Glu Tyr Thr Leu Thr Ile Ser Gly Val Gln Arg 65 70 75 80 Glu Asp Ala Ala Thr Tyr Tyr Cys Leu Gly Ser Leu Ser Asn Ser Asp 85 90 95 Asn Val Phe Gly Gly Gly Thr Glu Leu Glu Ile Leu 100 105 <210> 744 <211> 110 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 744 Glu Leu Val Met Thr Gln Thr Pro Ser Ser Thr Ser Gly Ala Val Gly 1 5 10 15 Gly Thr Val Thr Ile Asn Cys Gln Ala Ser Gln Ser Ile Asp Ser Asn 20 25 30 Leu Ala Trp Phe Gln Gln Lys Pro Gly Gln Pro Pro Thr Leu Leu Ile 35 40 45 Tyr Arg Ala Ser Asn Leu Ala Ser Gly Val Pro Ser Arg Phe Ser Gly 50 55 60 Ser Arg Ser Gly Thr Glu Tyr Thr Leu Thr Ile Ser Gly Val Gln Arg 65 70 75 80 Glu Asp Ala Ala Thr Tyr Tyr Cys Leu Gly Gly Val Gly Asn Val Ser 85 90 95 Tyr Arg Thr Ser Phe Gly Gly Gly Thr Glu Val Val Val Lys 100 105 110 <210> 745 <211> 113 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 745 Asp Ile Val Met Ser Gln Ser Pro Asp Ser Leu Ala Val Ser Leu Gly 1 5 10 15 Glu Arg Val Thr Leu Asn Cys Lys Ser Ser Gln Ser Leu Leu Tyr Ser 20 25 30 Gly Asn Gln Lys Asn Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln 35 40 45 Ser Pro Lys Leu Leu Ile Tyr Trp Ala Ser Ala Arg Glu Ser Gly Val 50 55 60 Pro Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr 65 70 75 80 Ile Ser Ser Val Gln Ala Glu Asp Val Ala Val Tyr Tyr Cys Gln Gln 85 90 95 Tyr Tyr Ser Tyr Pro Leu Thr Phe Gly Ala Gly Thr Lys Leu Glu Leu 100 105 110 Lys <210> 746 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 746 Ser Ile Val Met Thr Gln Thr Pro Lys Phe Leu Leu Val Ser Ala Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Lys Ala Ser Gln Ser Val Ser Asn Asp 20 25 30 Val Ala Trp Tyr Gln Gln Lys Pro Gly Gln Ser Pro Lys Leu Leu Ile 35 40 45 Asn Phe Ala Thr Asn Arg Tyr Thr Gly Val Pro Asn Arg Phe Thr Gly 50 55 60 Ser Gly Tyr Gly Thr Asp Phe Thr Phe Thr Ile Ser Thr Val Gln Ala 65 70 75 80 Glu Asp Leu Ala Leu Tyr Phe Cys Gln Gln Asp Tyr Ser Ser Pro Trp 85 90 95 Thr Phe Gly Gly Gly Thr Lys Leu Glu Ile Lys 100 105 <210> 747 <211> 115 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 747 Ser Val Ile Met Ser Arg Gly Gln Ile Val Leu Thr Gln Ser Pro Ala 1 5 10 15 Ile Met Ser Ala Ser Leu Gly Glu Arg Val Thr Leu Thr Cys Thr Ala 20 25 30 Ser Ser Ser Val Asn Ser Asn Tyr Leu His Trp Tyr Gln Gln Lys Pro 35 40 45 Gly Ser Ser Pro Lys Leu Trp Ile Tyr Ser Thr Ser Asn Leu Ala Ser 50 55 60 Gly Val Pro Ala Arg Phe Ser Gly Ser Gly Ser Gly Thr Ser Tyr Ser 65 70 75 80 Leu Thr Ile Ser Ser Met Glu Ala Glu Asp Ala Ala Thr Tyr Tyr Cys 85 90 95 His Gln Tyr His Arg Ser Pro Leu Thr Phe Gly Ala Gly Thr Lys Leu 100 105 110 Glu Leu Lys 115 <210> 748 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 748 Asp Ile Val Met Thr Gln Ser His Ile Phe Met Ser Thr Ser Val Gly 1 5 10 15 Asp Arg Val Ser Ile Thr Cys Lys Ala Ser Gln Asp Val Asp Thr Ala 20 25 30 Val Ala Trp Tyr Gln Gln Lys Pro Gly Gln Ser Pro Lys Leu Leu Ile 35 40 45 Tyr Trp Ala Ser Thr Arg Leu Thr Gly Val Pro Asp Arg Phe Thr Gly 50 55 60 Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Asn Val Gln Ser 65 70 75 80 Glu Asp Leu Ala Asp Tyr Phe Cys Gln Gln Tyr Ser Ser Tyr Pro Tyr 85 90 95 Thr Phe Gly Gly Gly Thr Lys Leu Glu Ile Lys 100 105 <210> 749 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 749 Asp Ile Gln Leu Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Ser Ile Thr Cys Lys Ala Ser Gln Asp Val Ser Ile Ala 20 25 30 Val Ala Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile 35 40 45 Tyr Ser Ala Ser Tyr Arg Tyr Thr Gly Val Pro Asp Arg Phe Ser Gly 50 55 60 Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Ser Leu Gln Pro 65 70 75 80 Glu Asp Phe Ala Val Tyr Tyr Cys Gln Gln His Tyr Ile Thr Pro Leu 85 90 95 Thr Phe Gly Ala Gly Thr Lys Val Glu Ile Lys 100 105 <210> 750 <211> 108 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 750 Glu Ile Val Leu Thr Gln Ser Pro Gly Thr Leu Ser Leu Ser Pro Gly 1 5 10 15 Glu Arg Ala Thr Leu Ser Cys Arg Ala Ser Gln Ser Val Ser Ser Ser 20 25 30 Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Gln Ala Pro Arg Leu Leu 35 40 45 Ile Tyr Gly Ala Ser Ser Arg Ala Thr Gly Ile Pro Asp Arg Phe Ser 50 55 60 Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile Ser Arg Leu Glu 65 70 75 80 Pro Glu Asp Phe Ala Val Tyr Tyr Cys Gln Gln Tyr Gly Ser Ser Pro 85 90 95 Leu Thr Phe Gly Gly Gly Thr Lys Val Glu Ile Lys 100 105 <210> 751 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 751 Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Val Ser Ala Ser Ile Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Arg Ala Ser Gln Gly Ile Asp Asn Trp 20 25 30 Leu Gly Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys Leu Leu Ile 35 40 45 Tyr Asp Ala Ser Asn Leu Asp Thr Gly Val Pro Ser Arg Phe Ser Gly 50 55 60 Ser Gly Ser Gly Thr Tyr Phe Thr Leu Thr Ile Ser Ser Leu Gln Ala 65 70 75 80 Glu Asp Phe Ala Val Tyr Phe Cys Gln Gln Ala Lys Ala Phe Pro Pro 85 90 95 Thr Phe Gly Gly Gly Thr Lys Val Asp Ile Lys 100 105 <210> 752 <211> 107 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 752 Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val Gly 1 5 10 15 Asp Arg Val Thr Ile Thr Cys Arg Ala Ser Gln Asp Ile Ala Gly Ser 20 25 30 Leu Asn Trp Leu Gln Gln Lys Pro Gly Lys Ala Ile Lys Arg Leu Ile 35 40 45 Tyr Ala Thr Ser Ser Leu Asp Ser Gly Val Pro Lys Arg Phe Ser Gly 50 55 60 Ser Arg Ser Gly Ser Asp Tyr Thr Leu Thr Ile Ser Ser Leu Gln Pro 65 70 75 80 Glu Asp Phe Ala Thr Tyr Tyr Cys Leu Gln Tyr Gly Ser Phe Pro Pro 85 90 95 Thr Phe Gly Gln Gly Thr Lys Val Glu Ile Lys 100 105 <210> 753 <211> 111 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 753 Asp Ile Val Leu Thr Gln Ser Pro Ala Ser Leu Ala Val Ser Leu Gly 1 5 10 15 Gln Arg Ala Thr Ile Ser Cys Arg Ala Ser Glu Ser Val Asp Ser Tyr 20 25 30 Gly Asn Ser Phe Met His Trp Tyr Gln Gln Lys Pro Gly Gln Pro Pro 35 40 45 Lys Leu Leu Ile Tyr Arg Ala Ser Asn Leu Glu Ser Gly Ile Pro Ala 50 55 60 Arg Phe Ser Gly Ser Gly Ser Arg Thr Asp Phe Thr Leu Thr Ile Asn 65 70 75 80 Pro Val Glu Ala Asp Asp Val Ala Thr Tyr Tyr Cys Gln Gln Ser Asn 85 90 95 Glu Asp Pro Leu Thr Phe Gly Ala Gly Thr Lys Leu Glu Leu Lys 100 105 110 <210> 754 <211> 117 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 754 Gln Ala Gln Leu Gln Val Ser Gly Ala Glu Val Val Lys Pro Gly Ala 1 5 10 15 Ser Val Lys Met Ser Cys Lys Ala Ser Gly Tyr Thr Phe Thr Ser Tyr 20 25 30 Asn Met His Trp Val Lys Gln Thr Pro Gly Gln Gly Leu Glu Trp Ile 35 40 45 Gly Tyr Ile Tyr Pro Gly Asn Gly Ala Thr Asn Tyr Asn Gln Lys Phe 50 55 60 Gln Gly Lys Ala Thr Leu Thr Ala Asp Thr Ser Ser Ser Thr Ala Tyr 65 70 75 80 Met Gln Ile Ser Ser Leu Thr Ser Glu Asp Ser Ala Val Tyr Phe Cys 85 90 95 Ala Arg Gly Asp Ser Val Pro Phe Ala Tyr Trp Gly Gln Gly Thr Leu 100 105 110 Val Thr Val Ser Ala 115 <210> 755 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 755 Gly Pro Pro Gly Lys Asn Gly Glu 1 5 <210> 756 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 756 Val Glu Asn Ala Lys Thr Phe Gly 1 5 <210> 757 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 757 Gly Ala Ala Gly Val Lys Gly Asp 1 5 <210> 758 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 758 Ser Leu Met Lys Arg Pro Pro Gly 1 5 <210> 759 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 759 Asn Gly Phe Lys Ser His Ala Leu 1 5 <210> 760 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 760 Ser Leu Met Lys Arg Pro Pro Gly 1 5 <210> 761 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 761 Thr His Arg Ile His Trp Glu Ser 1 5 <210> 762 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 762 Ser Ser Lys Ile Thr His Arg Ile 1 5 <210> 763 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 763 Lys Ser His Ala Leu Gln Leu Asn 1 5 <210> 764 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 764 Ile Thr His Arg Ile His Trp Glu 1 5 <210> 765 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 765 Phe Lys Ser His Ala Leu Gln Leu 1 5 <210> 766 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 766 Arg Ser Ser Lys Ile Thr His Arg 1 5 <210> 767 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 767 Pro Val Ser Ala Met Glu Pro Leu 1 5 <210> 768 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 768 Gly His Thr Arg Arg His Asp Trp 1 5 <210> 769 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 769 Lys Ile Thr His Arg Ile His Trp 1 5 <210> 770 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 770 Ser Arg Ser Ser Lys Ile Thr His 1 5 <210> 771 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 771 Arg Gln Ile Arg Gly Leu Glu Glu 1 5 <210> 772 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 772 Asn Gly Phe Lys Ser His Ala Leu 1 5 <210> 773 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 773 Pro Ser Arg Ser Ser Lys Ile Thr 1 5 <210> 774 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 774 Ser Thr Gly Arg Asn Gly Phe Lys 1 5 <210> 775 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 775 Leu Pro His Arg Arg Pro His Phe 1 5 <210> 776 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 776 Asn Asn Pro Val Pro Tyr Trp Glu Val Gln 1 5 10 <210> 777 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 777 Gly Leu Pro Tyr Thr Thr Gly Lys Leu Pro 1 5 10 <210> 778 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 778 Ala Arg Pro Gly Phe Gly Leu Ser Pro Ile 1 5 10 <210> 779 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 779 Ser Arg Gly Lys Ser Ser Ser Tyr 1 5 <210> 780 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 780 Ser Arg Gly Lys Ser Ser Ser Tyr 1 5 <210> 781 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 781 Asp Gly Phe Arg His Arg His Pro 1 5 <210> 782 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 782 Ser Arg Gly Lys Ser Ser Ser Tyr 1 5 <210> 783 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 783 Thr Ala Trp Thr Ala Asp Ser Gly 1 5 <210> 784 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 784 Ala Trp Thr Ala Asp Ser Gly Glu 1 5 <210> 785 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 785 Ala Trp Thr Ala Asp Ser Gly Glu 1 5 <210> 786 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 786 Lys Asn Asn Lys Asp Ser His Ser 1 5 <210> 787 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 787 Trp Thr Ala Asp Ser Gly Glu Gly 1 5 <210> 788 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 788 Gly Gly Val Arg Gly Pro Arg Val 1 5 <210> 789 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 789 Ser Arg Gly Lys Ser Ser Ser Tyr 1 5 <210> 790 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 790 Thr Ala Trp Thr Ala Asp Ser Gly 1 5 <210> 791 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 791 Gly Asn Phe Lys Ser Gln Leu Gln 1 5 <210> 792 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 792 Thr Ala Asp Ser Gly Glu Gly Asp 1 5 <210> 793 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 793 Ser Ser Gly Pro Gly Ser Thr Gly 1 5 <210> 794 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 794 Ala Asp Ser Gly Glu Gly Asp Phe 1 5 <210> 795 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 795 Ser Arg Gly Lys Ser Ser Ser Tyr 1 5 <210> 796 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 796 Ser Arg Gly Lys Ser Ser Ser Tyr 1 5 <210> 797 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 797 Thr Ala Trp Thr Ala Asp Ser Gly 1 5 <210> 798 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 798 Asn Phe Lys Ser Gln Leu Gln Lys 1 5 <210> 799 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 799 Lys Met Lys Pro Val Pro Asp Leu 1 5 <210> 800 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 800 Ser Gly Glu Gly Asp Phe Leu Ala 1 5 <210> 801 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 801 Thr Ala Trp Thr Ala Asp Ser Gly 1 5 <210> 802 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 802 Ser Thr Gly Lys Thr Phe Pro Gly 1 5 <210> 803 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 803 Pro Leu Ile Lys Met Lys Pro Val 1 5 <210> 804 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 804 Pro Leu Ile Lys Met Lys Pro Val 1 5 <210> 805 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 805 Gly Ser Trp Asn Ser Gly Ser Ser 1 5 <210> 806 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 806 Pro Leu Ile Lys Met Lys Pro Val 1 5 <210> 807 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 807 Gly Glu Phe Val Ser Glu Thr Glu 1 5 <210> 808 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 808 Ala Trp Thr Ala Asp Ser Gly Glu 1 5 <210> 809 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 809 Lys Asn Asn Lys Asp Ser His Ser 1 5 <210> 810 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 810 Thr Ala Trp Thr Ala Asp Ser Gly 1 5 <210> 811 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 811 Pro Leu Ile Lys Met Lys Pro Val 1 5 <210> 812 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 812 Gly Gln Trp His Ser Glu Ser Gly 1 5 <210> 813 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 813 Lys Met Lys Pro Val Pro Asp Leu 1 5 <210> 814 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 814 Met Arg Met Glu Leu Glu Arg Pro 1 5 <210> 815 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 815 Lys Pro Val Pro Asp Leu Val Pro 1 5 <210> 816 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 816 Pro Leu Ile Lys Met Lys Pro Val 1 5 <210> 817 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 817 Thr Ala Trp Thr Ala Asp Ser Gly 1 5 <210> 818 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 818 Gly Asn Phe Lys Ser Gln Leu Gln 1 5 <210> 819 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 819 Arg Gly Lys Ser Ser Ser Tyr Ser 1 5 <210> 820 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 820 Met Leu Gly Glu Phe Val Ser Glu 1 5 <210> 821 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 821 Met Arg Met Glu Leu Glu Arg Pro 1 5 <210> 822 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 822 Ser Tyr Ser Lys Gln Phe Thr Ser 1 5 <210> 823 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 823 Glu Ser Ser Val Ser Gly Ser Thr 1 5 <210> 824 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 824 Asp Gly Phe Arg His Arg His Pro 1 5 <210> 825 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 825 Pro Leu Ile Lys Met Lys Pro Val 1 5 <210> 826 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 826 Trp Gly Thr Phe Glu Glu Val Ser 1 5 <210> 827 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 827 Met Arg Met Glu Leu Glu Arg Pro 1 5 <210> 828 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 828 Glu Ala Ala Phe Phe Asp Thr Ala 1 5 <210> 829 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 829 Ser Arg Gly Lys Ser Ser Ser Tyr 1 5 <210> 830 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 830 Pro Leu Ile Lys Met Lys Pro Val 1 5 <210> 831 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 831 Asp Pro Gln Gly Asp Ala Ala Gln 1 5 <210> 832 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 832 Phe Val Phe Leu Met Ile Glu Gln 1 5 <210> 833 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 833 Met Phe Leu Glu Ala Ile Pro Met 1 5 <210> 834 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 834 Ile Pro Met Ser Ile Pro Pro Glu 1 5 <210> 835 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 835 Gly Thr Glu Ala Ala Gly Ala Met 1 5 <210> 836 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 836 Ala Ile Pro Met Ser Ile Pro Pro 1 5 <210> 837 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 837 Pro Phe Val Phe Leu Met Ile Glu 1 5 <210> 838 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 838 Pro Glu Val Lys Phe Asn Lys Pro 1 5 <210> 839 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 839 Ala Met Phe Leu Glu Ala Ile Pro 1 5 <210> 840 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 840 Val Ser Leu Ala Glu Asp Pro Gln 1 5 <210> 841 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 841 Val Phe Leu Met Ile Glu Gln Asn 1 5 <210> 842 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 842 Ala Ala Gly Ala Met Phe Leu Glu 1 5 <210> 843 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 843 Glu Ala Ile Pro Met Ser Ile Pro 1 5 <210> 844 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 844 Ala Gly Ala Met Phe Leu Glu Ala 1 5 <210> 845 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 845 Asp Pro Gln Gly Asp Ala Ala Gln 1 5 <210> 846 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 846 Asp Glu Lys Gly Thr Glu Ala Ala 1 5 <210> 847 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 847 Glu Lys Gly Thr Glu Ala Ala Gly 1 5 <210> 848 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 848 Ala Met Phe Leu Glu Ala Ile Pro 1 5 <210> 849 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 849 Val Ser Leu Ala Glu Asp Pro Gln 1 5 <210> 850 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 850 Val Ser Leu Ala Glu Asp Pro Gln 1 5 <210> 851 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 851 Lys Gly Thr Glu Ala Ala Gly Ala 1 5 <210> 852 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 852 Asp Pro Gln Gly Asp Ala Ala Gln 1 5 <210> 853 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 853 Thr Glu Ala Ala Gly Ala Met Phe 1 5 <210> 854 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 854 Ile Asp Glu Lys Gly Thr Glu Ala 1 5 <210> 855 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 855 Glu Ala Ala Gly Ala Met Phe Leu 1 5 <210> 856 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 856 Val Ser Leu Ala Glu Asp Pro Gln 1 5 <210> 857 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 857 Leu Ala Glu Asp Pro Gln Gly Asp 1 5 <210> 858 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 858 Leu Ser Leu Gln Lys Pro Arg Leu 1 5 <210> 859 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 859 Leu Ser Leu Gln Lys Pro Arg Leu 1 5 <210> 860 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 860 Leu Ser Leu Gln Lys Pro Arg Leu 1 5 <210> 861 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 861 Leu Ser Leu Gln Lys Pro Arg Leu 1 5 <210> 862 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 862 Leu Ser Leu Gln Lys Pro Arg Leu 1 5 <210> 863 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 863 Leu Ser Leu Gln Lys Pro Arg Leu 1 5 <210> 864 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 864 Leu Ser Leu Gln Lys Pro Arg Leu 1 5 <210> 865 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 865 Leu Ser Leu Gln Lys Pro Arg Leu 1 5 <210> 866 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 866 Ser Thr Gly Arg Asn Gly Phe Lys 1 5 <210> 867 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 867 Leu Ser Leu Gln Lys Pro Arg Leu 1 5 <210> 868 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 868 Ser Thr Gly Arg Asn Gly Phe Lys 1 5 <210> 869 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 869 Leu Pro Ala Lys Asp Asp Pro Asp 1 5 <210> 870 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 870 Leu Ser Leu Gln Lys Pro Arg Leu 1 5 <210> 871 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 871 Arg Gln Ile Arg Gly Leu Glu Glu 1 5 <210> 872 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 872 Pro Ala Lys Asp Asp Pro Asp Ala 1 5 <210> 873 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 873 Leu Pro Ala Lys Asp Asp Pro Asp 1 5 <210> 874 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 874 Thr Gly Arg Asn Gly Phe Lys Ser 1 5 <210> 875 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 875 Leu Pro Ala Lys Asp Asp Pro Asp 1 5 <210> 876 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 876 Leu Ser Leu Gln Lys Pro Arg Leu 1 5 <210> 877 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 877 Leu Pro Ala Lys Asp Asp Pro Asp 1 5 <210> 878 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 878 Arg Gln Ile Arg Gly Leu Glu Glu 1 5 <210> 879 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 879 His Arg Gly Arg Thr Leu Glu Ile 1 5 <210> 880 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 880 Pro Arg Leu Leu Leu Phe Ser Pro 1 5 <210> 881 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 881 Ser Glu Leu Gln Leu Ser Val Ser 1 5 <210> 882 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 882 Ala Arg Leu Thr Val Ala Ala Pro 1 5 <210> 883 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 883 Pro Arg Leu Leu Leu Phe Ser Pro 1 5 <210> 884 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 884 Ala Lys Asp Asp Pro Asp Ala Pro 1 5 <210> 885 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 885 Pro Ala Lys Asp Asp Pro Asp Ala 1 5 <210> 886 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 886 Arg Leu Leu Leu Phe Ser Pro Ser 1 5 <210> 887 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 887 Asp Tyr Glu Tyr Asp Glu Leu Pro 1 5 <210> 888 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 888 Pro Arg Leu Leu Leu Phe Ser Pro 1 5 <210> 889 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 889 Pro Arg Leu Leu Leu Phe Ser Pro 1 5 <210> 890 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 890 Leu Thr Val Ala Ala Pro Pro Ser 1 5 <210> 891 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 891 Asp Lys Lys Arg Glu Glu Ala Pro 1 5 <210> 892 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 892 Lys Lys Arg Glu Glu Ala Pro Ser 1 5 <210> 893 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 893 Leu Asp Lys Lys Arg Glu Glu Ala 1 5 <210> 894 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 894 Leu Val Lys Ser Gln Gly Val Asn 1 5 <210> 895 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 895 Leu Val Lys Ser Gln Gly Val Asn 1 5 <210> 896 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 896 Leu Val Lys Ser Gln Gly Val Asn 1 5 <210> 897 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 897 Leu Val Lys Ser Gln Gly Val Asn 1 5 <210> 898 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 898 Leu Val Lys Ser Gln Gly Val Asn 1 5 <210> 899 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 899 Pro Leu Asp Lys Lys Arg Glu Glu 1 5 <210> 900 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 900 Leu Val Lys Ser Gln Gly Val Asn 1 5 <210> 901 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 901 Leu Val Lys Ser Gln Gly Val Asn 1 5 <210> 902 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 902 His Arg Pro Leu Asp Lys Lys Arg 1 5 <210> 903 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 903 Leu Val Lys Ser Gln Gly Val Asn 1 5 <210> 904 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 904 Ser Gln Gly Val Asn Asp Asn Glu 1 5 <210> 905 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 905 Leu Val Lys Ser Gln Gly Val Asn 1 5 <210> 906 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 906 Leu Val Lys Ser Gln Gly Val Asn 1 5 <210> 907 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 907 Lys Ser Gln Gly Val Asn Asp Asn 1 5 <210> 908 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 908 Lys Ser Gln Gly Val Asn Asp Asn 1 5 <210> 909 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 909 Lys Ser Gln Gly Val Asn Asp Asn 1 5 <210> 910 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 910 Leu Val Lys Ser Gln Gly Val Asn 1 5 <210> 911 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 911 Leu Val Lys Ser Gln Gly Val Asn 1 5 <210> 912 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 912 Leu Val Lys Ser Gln Gly Val Asn 1 5 <210> 913 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 913 Lys Ser Gln Gly Val Asn Asp Asn 1 5 <210> 914 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 914 Pro Leu Asp Lys Lys Arg Glu Glu 1 5 <210> 915 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 915 Phe Ser Ala Arg Gly His Arg Pro 1 5 <210> 916 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 916 Ser Gln Gly Val Asn Asp Asn Glu 1 5 <210> 917 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 917 Leu Val Lys Ser Gln Gly Val Asn 1 5 <210> 918 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 918 Leu Val Lys Ser Gln Gly Val Asn 1 5 <210> 919 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 919 Met Ser Met Lys Ile Arg Pro Phe 1 5 <210> 920 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 920 Gln Gly Val Asn Asp Asn Glu Glu 1 5 <210> 921 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 921 Leu Val Lys Ser Gln Gly Val Asn 1 5 <210> 922 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 922 Leu Val Lys Ser Gln Gly Val Asn 1 5 <210> 923 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 923 Leu Val Lys Ser Gln Gly Val Asn 1 5 <210> 924 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 924 Asn Ile Gln Arg Phe Phe Gly His 1 5 <210> 925 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 925 Ala Ala Glu Ala Ile Ser Asp Ala 1 5 <210> 926 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 926 Gly Ala Glu Asp Ser Leu Ala Asp 1 5 <210> 927 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 927 Ile Gln Arg Phe Phe Gly His Gly 1 5 <210> 928 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 928 Gly Val Ser Ser Arg Ser Phe Phe 1 5 <210> 929 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 929 Ser Gly Lys Asp Pro Asn His Phe 1 5 <210> 930 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 930 Gly Val Trp Ala Ala Glu Ala Ile 1 5 <210> 931 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 931 Ala Asp Gln Ala Ala Asn Glu Trp 1 5 <210> 932 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 932 Gly Glu Ala Phe Asp Gly Ala Arg 1 5 <210> 933 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 933 Ala Ile Ser Asp Ala Arg Glu Asn 1 5 <210> 934 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 934 Val Ser Ser Arg Ser Phe Phe Ser 1 5 <210> 935 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 935 Glu Ala Phe Asp Gly Ala Arg Asp 1 5 <210> 936 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 936 Asp Ser Leu Ala Asp Gln Ala Ala 1 5 <210> 937 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 937 Ser Phe Phe Ser Phe Leu Gly Glu 1 5 <210> 938 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 938 Ser Leu Ala Asp Gln Ala Ala Asn 1 5 <210> 939 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 939 Glu Asn Ile Gln Arg Phe Phe Gly 1 5 <210> 940 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 940 Asn Ile Gln Arg Phe Phe Gly His 1 5 <210> 941 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 941 Phe Phe Gly His Gly Ala Glu Asp 1 5 <210> 942 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 942 Arg Ser Gly Lys Asp Pro Asn His 1 5 <210> 943 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 943 Arg Phe Phe Gly His Gly Ala Glu 1 5 <210> 944 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 944 Glu Trp Gly Arg Ser Gly Lys Asp 1 5 <210> 945 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 945 Asp Gln Ala Ala Asn Glu Trp Gly 1 5 <210> 946 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 946 Glu Ala Ile Ser Asp Ala Arg Glu 1 5 <210> 947 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 947 Arg Ser Phe Phe Ser Phe Leu Gly 1 5 <210> 948 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 948 Asp Ser Leu Ala Asp Gln Ala Ala 1 5 <210> 949 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 949 Ala Ile Ser Asp Ala Arg Glu Asn 1 5 <210> 950 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 950 Glu Asp Ser Leu Ala Asp Gln Ala 1 5 <210> 951 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 951 Ala Glu Ala Ile Ser Asp Ala Arg 1 5 <210> 952 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 952 Phe Ser Phe Leu Gly Glu Ala Phe 1 5 <210> 953 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 953 Phe His Ala Arg Gly Asn Tyr Asp 1 5 <210> 954 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 954 Gly Val Ser Ser Arg Ser Phe Phe 1 5 <210> 955 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 955 Lys Arg Gly Pro Gly Gly Val Trp 1 5 <210> 956 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 956 Phe Thr Ala Asn Asp Ser Gly Pro 1 5 <210> 957 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 957 Ala Asn Asp Ser Gly Pro Arg Arg 1 5 <210> 958 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 958 Ala Asn Asp Ser Gly Pro Arg Arg 1 5 <210> 959 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 959 Thr Ala Asn Asp Ser Gly Pro Arg 1 5 <210> 960 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 960 Asn Asp Ser Gly Pro Arg Arg Tyr 1 5 <210> 961 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 961 Ala Ala Leu Leu Ser Pro Tyr Ser 1 5 <210> 962 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 962 Tyr Thr Ile Ala Ala Leu Leu Ser 1 5 <210> 963 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 963 Arg Arg Tyr Thr Ile Ala Ala Leu 1 5 <210> 964 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 964 Glu Val Val Phe Thr Ala Asn Asp 1 5 <210> 965 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 965 Lys Ala Leu Gly Ile Ser Pro Phe 1 5 <210> 966 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 966 Pro Val Ser Ala Met Glu Pro Leu 1 5 <210> 967 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 967 Pro Val Ser Ala Met Glu Pro Leu 1 5 <210> 968 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 968 Thr Ser Gly Pro Asn Gln Glu Gln 1 5 <210> 969 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 969 Pro Asp Leu Lys Leu Val Pro Pro 1 5 <210> 970 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 970 Arg Gln Leu Thr Ser Gly Pro Asn 1 5 <210> 971 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 971 Pro Val Ser Ala Met Glu Pro Leu 1 5 <210> 972 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 972 Val Ser Ala Met Glu Pro Leu Gly 1 5 <210> 973 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 973 Thr Ser Gly Pro Asn Gln Glu Gln 1 5 <210> 974 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 974 Thr Ser Gly Pro Asn Gln Glu Gln 1 5 <210> 975 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 975 Ala Met Ser Arg Met Ser Leu Ser 1 5 <210> 976 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 976 Pro Val Ser Ala Met Glu Pro Leu 1 5 <210> 977 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 977 Leu Leu Pro Val Leu Glu Ser Phe 1 5 <210> 978 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 978 Leu Pro Val Leu Glu Ser Phe Lys 1 5 <210> 979 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 979 Arg Val Lys Asp Leu Ala Thr Val 1 5 <210> 980 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 980 Phe Trp Gln Gln Asp Glu Pro Pro 1 5 <210> 981 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 981 Pro Val Leu Glu Ser Phe Lys Val 1 5 <210> 982 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 982 Glu Ser Phe Lys Val Ser Phe Leu 1 5 <210> 983 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 983 Glu Phe Trp Asp Asn Leu Glu Lys 1 5 <210> 984 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 984 Val Ser Phe Leu Ser Ala Leu Glu 1 5 <210> 985 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 985 Ser Phe Lys Val Ser Phe Leu Ser 1 5 <210> 986 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 986 Phe Trp Gln Gln Asp Glu Pro Pro 1 5 <210> 987 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 987 Glu Pro Leu Arg Ala Glu Leu Gln 1 5 <210> 988 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 988 Glu Pro Leu Arg Ala Glu Leu Gln 1 5 <210> 989 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 989 Phe Trp Gln Gln Asp Glu Pro Pro 1 5 <210> 990 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 990 Leu Leu Ser Ala Leu Val Glu Thr 1 5 <210> 991 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 991 Ile Thr Leu Leu Ser Ala Leu Val 1 5 <210> 992 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 992 Leu Ser Ala Leu Val Glu Thr Arg 1 5 <210> 993 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 993 Ala Leu Val Glu Thr Arg Thr Ile 1 5 <210> 994 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 994 Val Pro Thr Asp Thr Gln Asn Ile 1 5 <210> 995 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 995 Thr Leu Leu Ser Ala Leu Val Glu 1 5 <210> 996 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 996 Leu Cys His Pro Asn Ser Pro Leu 1 5 <210> 997 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 997 Pro Phe Leu Met Ile Ile Val Pro 1 5 <210> 998 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 998 Ala Val Leu Cys His Pro Asn Ser 1 5 <210> 999 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 999 Gly Ser Trp Gln Arg Ser Leu Gln 1 5 <210> 1000 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1000 Gly Ser Trp Gln Arg Ser Leu Gln 1 5 <210> 1001 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1001 Trp Gln Arg Ser Leu Gln Asp Thr 1 5 <210> 1002 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1002 Ser Trp Gln Arg Ser Leu Gln Asp 1 5 <210> 1003 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1003 Glu Asp Lys Arg His Ser Gln Gly 1 5 <210> 1004 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1004 Trp Gln Arg Ser Leu Gln Asp Thr 1 5 <210> 1005 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1005 Glu Asp Lys Arg His Ser Gln Gly 1 5 <210> 1006 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1006 Gln Arg Ser Leu Gln Asp Thr Glu 1 5 <210> 1007 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1007 Ser Trp Gln Arg Ser Leu Gln Asp 1 5 <210> 1008 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1008 Arg Gly Arg Arg Asp Phe Pro Glu 1 5 <210> 1009 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1009 Ile Ala Lys Arg His Asp Glu Phe 1 5 <210> 1010 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1010 Leu Thr Ser Gly Ser Val Phe Pro 1 5 <210> 1011 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1011 Leu Thr Ser Gly Ser Val Phe Pro 1 5 <210> 1012 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1012 Leu Thr Ser Gly Ser Val Phe Pro 1 5 <210> 1013 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1013 Leu Thr Ser Gly Ser Val Phe Pro 1 5 <210> 1014 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1014 Leu Thr Ser Gly Ser Val Phe Pro 1 5 <210> 1015 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1015 Leu Thr Ser Gly Ser Val Phe Pro 1 5 <210> 1016 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1016 Ser Val Phe Pro Gln Gln Thr Gly 1 5 <210> 1017 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1017 Thr Ser Gly Ser Val Phe Pro Gln 1 5 <210> 1018 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1018 Ser Val Phe Pro Gln Gln Thr Gly 1 5 <210> 1019 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1019 Leu Thr Ser Gly Ser Val Phe Pro 1 5 <210> 1020 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1020 Leu Thr Ser Gly Ser Val Phe Pro 1 5 <210> 1021 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1021 Leu Thr Ser Gly Ser Val Phe Pro 1 5 <210> 1022 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1022 Asn Ile Gln Arg Leu Thr Gly Arg 1 5 <210> 1023 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1023 Ile Gln Arg Leu Thr Gly Arg Gly 1 5 <210> 1024 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1024 Arg Ser Gly Arg Asp Pro Asn His 1 5 <210> 1025 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1025 Gln Arg Leu Thr Gly Arg Gly Ala 1 5 <210> 1026 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1026 Ile Gln Arg Leu Thr Gly Arg Gly 1 5 <210> 1027 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1027 Asn Ile Gln Arg Leu Thr Gly Arg 1 5 <210> 1028 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1028 Gly Ala Glu Asp Ser Leu Ala Asp 1 5 <210> 1029 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1029 Arg Leu Thr Gly Arg Gly Ala Glu 1 5 <210> 1030 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1030 Thr Gly Arg Gly Ala Glu Asp Ser 1 5 <210> 1031 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1031 Ala Ala Lys Arg Gly Pro Gly Gly 1 5 <210> 1032 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1032 Gly Ala Trp Ala Ala Glu Val Ile 1 5 <210> 1033 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1033 Asp Ser Leu Ala Asp Gln Ala Ala 1 5 <210> 1034 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1034 Ala Trp Ala Ala Glu Val Ile Ser 1 5 <210> 1035 <211> 5 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1035 Met Ser Asp Lys Pro 1 5 <210> 1036 <211> 5 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1036 Met Ser Asp Lys Pro 1 5 <210> 1037 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1037 Lys Thr Glu Thr Gln Glu Lys Asn 1 5 <210> 1038 <211> 5 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1038 Met Ser Asp Lys Pro 1 5 <210> 1039 <211> 5 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1039 Met Ser Asp Lys Pro 1 5 <210> 1040 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1040 Lys Lys Thr Glu Thr Gln Glu Lys 1 5 <210> 1041 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1041 Glu Thr Gln Glu Lys Asn Pro Leu 1 5 <210> 1042 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1042 Lys Leu Lys Lys Thr Glu Thr Gln 1 5 <210> 1043 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1043 Thr Glu Thr Gln Glu Lys Asn Pro 1 5 <210> 1044 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1044 Thr Gln Glu Lys Asn Pro Leu Pro 1 5 <210> 1045 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1045 Pro Val Gln Arg Ile Leu Gly Gly 1 5 <210> 1046 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1046 Pro Val Gln Arg Ile Leu Gly Gly 1 5 <210> 1047 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1047 Gly Val Tyr Val Lys Val Thr Ser 1 5 <210> 1048 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1048 Pro Val Gln Arg Ile Leu Gly Gly 1 5 <210> 1049 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1049 Pro Val Gln Arg Ile Leu Gly Gly 1 5 <210> 1050 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1050 Ser Ala Leu Gly Ala Val Ile Ala 1 5 <210> 1051 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1051 Met Ser Ala Leu Gly Ala Val Ile 1 5 <210> 1052 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1052 His Cys Leu Leu Val Thr Leu Ala 1 5 <210> 1053 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1053 Leu Leu Val Thr Leu Ala Ala His 1 5 <210> 1054 <211> 5 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1054 Met Val Leu Ser Pro 1 5 <210> 1055 <211> 5 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1055 Met Val Leu Ser Pro 1 5 <210> 1056 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1056 Ala Ser Leu Asp Lys Phe Leu Ala 1 5 <210> 1057 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1057 Leu Val Thr Leu Ala Ala His Leu 1 5 <210> 1058 <211> 5 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1058 Met Val Leu Ser Pro 1 5 <210> 1059 <211> 5 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1059 Met Val Leu Ser Pro 1 5 <210> 1060 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1060 Gln Lys Val Arg Tyr Glu Gly Ser 1 5 <210> 1061 <211> 5 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1061 Met Gly Glu Asp Ala 1 5 <210> 1062 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1062 Glu Gly Ser Tyr Ala Leu Thr Ser 1 5 <210> 1063 <211> 5 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1063 Met Gly Glu Asp Ala 1 5 <210> 1064 <211> 5 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1064 Met Gly Glu Asp Ala 1 5 <210> 1065 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1065 Arg Tyr Glu Gly Ser Tyr Ala Leu 1 5 <210> 1066 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1066 Pro Pro Leu Gly Ala Pro Gly Leu 1 5 <210> 1067 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1067 Arg Lys Thr Arg Thr Val Val Gln 1 5 <210> 1068 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1068 Pro Pro Leu Gly Ala Pro Gly Leu 1 5 <210> 1069 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1069 His Val Leu Leu Ala Ala Pro Pro 1 5 <210> 1070 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1070 Pro Pro Leu Gly Ala Pro Gly Leu 1 5 <210> 1071 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1071 Val Leu Leu Ala Ala Pro Pro Gly 1 5 <210> 1072 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1072 Pro Pro Leu Gly Ala Pro Gly Leu 1 5 <210> 1073 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1073 His Val Leu Leu Ala Ala Pro Pro 1 5 <210> 1074 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1074 Gln Gln Lys Lys His Ser Gly Phe 1 5 <210> 1075 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1075 Gln Gln Lys Lys His Ser Gly Phe 1 5 <210> 1076 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1076 Leu Gln Val Arg Gly Tyr Pro Glu 1 5 <210> 1077 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1077 Gln Gln Lys Lys His Ser Gly Phe 1 5 <210> 1078 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1078 Ala Glu Lys Arg Leu Glu Gly Gln 1 5 <210> 1079 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1079 Ala Glu Lys Arg Leu Glu Gly Gln 1 5 <210> 1080 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1080 Leu Pro Ser Arg Ser Ser Lys Ile 1 5 <210> 1081 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1081 Leu Pro Ser Arg Ser Ser Lys Ile 1 5 <210> 1082 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1082 Ser Ser Lys Ile Thr His Arg Ile 1 5 <210> 1083 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1083 Ser Arg Ser Ser Lys Ile Thr His 1 5 <210> 1084 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1084 Leu Ala Leu Gly Ser Pro Met Tyr 1 5 <210> 1085 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1085 Lys Ile Thr His Arg Ile His Trp 1 5 <210> 1086 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1086 Ser Lys Ile Thr His Arg Ile His 1 5 <210> 1087 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1087 Thr His Arg Ile His Trp Glu Ser 1 5 <210> 1088 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1088 Ile Thr His Arg Ile His Trp Glu 1 5 <210> 1089 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1089 Phe Trp Gly Arg Thr Ser Ala Gly 1 5 <210> 1090 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1090 Thr Ser Ala Gly Thr Arg Gln Pro 1 5 <210> 1091 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1091 Leu Thr Ser Asp Leu Gln Ala Gln 1 5 <210> 1092 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1092 Phe Glu Leu Leu Phe Trp Gly Arg 1 5 <210> 1093 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1093 Thr Ser Ala Gly Thr Arg Gln Pro 1 5 <210> 1094 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1094 Phe Trp Gly Arg Thr Ser Ala Gly 1 5 <210> 1095 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1095 Phe Glu Leu Leu Phe Trp Gly Arg 1 5 <210> 1096 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1096 Gln Gly His Asn Ser Val Phe Leu 1 5 <210> 1097 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1097 Gln Gly His Asn Ser Val Phe Leu 1 5 <210> 1098 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1098 Gln Gly His Asn Ser Val Phe Leu 1 5 <210> 1099 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1099 Arg Trp Lys Asn Phe Pro Ser Pro 1 5 <210> 1100 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1100 Gln Gly His Asn Ser Val Phe Leu 1 5 <210> 1101 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1101 Asp Lys Val Trp Val Tyr Pro Pro 1 5 <210> 1102 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1102 Gln Thr Gln Phe His Val Gln Pro 1 5 <210> 1103 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1103 Gln Pro Val Ser Leu Ala Asn Thr 1 5 <210> 1104 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1104 Gln Thr Gln Phe His Val Gln Pro 1 5 <210> 1105 <211> 5 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1105 Met Ala Ala Pro Arg 1 5 <210> 1106 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1106 Gln Thr Gln Phe His Val Gln Pro 1 5 <210> 1107 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1107 Pro Lys Pro Lys Val Asn Pro Phe 1 5 <210> 1108 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1108 Ser Ala Arg Ala Ser Glu Ala Glu 1 5 <210> 1109 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1109 Ser Ala Arg Ala Ser Glu Ala Glu 1 5 <210> 1110 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1110 Phe Ser Glu Phe Trp Asp Leu Asp 1 5 <210> 1111 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1111 Ser Ala Arg Ala Ser Glu Ala Glu 1 5 <210> 1112 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1112 Trp Asp Leu Asp Pro Glu Val Arg 1 5 <210> 1113 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1113 Lys Arg Phe Pro Val Gly Pro Pro 1 5 <210> 1114 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1114 Val Ser Lys Arg Phe Pro Val Gly 1 5 <210> 1115 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1115 Lys Arg Phe Pro Val Gly Pro Pro 1 5 <210> 1116 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1116 Lys Arg Val Pro Gly Gln Gly Ser 1 5 <210> 1117 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1117 Gln Val Lys Arg Val Pro Gly Gln 1 5 <210> 1118 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1118 Pro Lys Thr Pro Gly Arg Ala Gly 1 5 <210> 1119 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1119 Glu Arg Lys Leu Lys His Met Gln 1 5 <210> 1120 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1120 Gln Gln Leu Asn Lys Pro Glu Val 1 5 <210> 1121 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1121 Glu Pro Thr Glu Ser Thr Gln Gln 1 5 <210> 1122 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1122 Thr Glu Ser Thr Gln Gln Leu Asn 1 5 <210> 1123 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1123 His Ala Phe Gly Gln Thr Asp Met 1 5 <210> 1124 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1124 His Ala Phe Gly Gln Thr Asp Met 1 5 <210> 1125 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1125 His Ala Phe Gly Gln Thr Asp Met 1 5 <210> 1126 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1126 Val Phe Arg Arg Asp Ala His Lys 1 5 <210> 1127 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1127 Val Phe Arg Arg Asp Ala His Lys 1 5 <210> 1128 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1128 Val Phe Arg Arg Asp Ala His Lys 1 5 <210> 1129 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1129 Gly Leu Gln Met Gly Thr Asn Arg 1 5 <210> 1130 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1130 Ile Gly Leu Gln Met Gly Thr Asn 1 5 <210> 1131 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1131 Gln Ala Gly Met Thr Gly Tyr Gly 1 5 <210> 1132 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1132 Tyr Gly Lys Arg His Lys Glu Asp 1 5 <210> 1133 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1133 Gln Gly Ala Pro Leu Glu Pro Val 1 5 <210> 1134 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1134 Pro Leu Leu Gly Ala Gln Gly Ala 1 5 <210> 1135 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1135 Gln Gly Ala Pro Leu Glu Pro Val 1 5 <210> 1136 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1136 Ala Ala Pro Pro Gly Arg Pro Glu 1 5 <210> 1137 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1137 Ala Ala Pro Pro Gly Arg Pro Glu 1 5 <210> 1138 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1138 Gly Leu Gly Ala Ala Pro Pro Gly 1 5 <210> 1139 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1139 Arg Lys Lys Asn Ala Pro Pro Glu 1 5 <210> 1140 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1140 Lys Arg Lys Lys Asn Ala Pro Pro 1 5 <210> 1141 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1141 Gly Leu Gly Ala Ala Pro Pro Gly 1 5 <210> 1142 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1142 Glu Glu Glu Ala Ala Glu Ala Leu 1 5 <210> 1143 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1143 Lys Arg Lys Lys Asn Ala Pro Pro 1 5 <210> 1144 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1144 Leu Leu His Cys His Val Thr Asp 1 5 <210> 1145 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1145 Pro Ala Trp Ala Lys Glu Lys His 1 5 <210> 1146 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1146 Pro Phe Thr Ala Ser Pro Ala Ser 1 5 <210> 1147 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1147 Leu Val Leu Gln Glu Ile Leu Glu 1 5 <210> 1148 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1148 Thr Asn Gln Tyr Asn Asn Pro Ala 1 5 <210> 1149 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1149 Phe Pro Leu Ala Thr Tyr Ala Pro 1 5 <210> 1150 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1150 Phe Pro Leu Ala Thr Tyr Ala Pro 1 5 <210> 1151 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1151 Pro Val Ile Ser Ala Glu Lys Ala 1 5 <210> 1152 <211> 5 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1152 Met Val His Leu Thr 1 5 <210> 1153 <211> 5 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1153 Met Val His Leu Thr 1 5 <210> 1154 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1154 Leu Gly Arg Leu Leu Val Val Tyr 1 5 <210> 1155 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1155 Ser Leu Asn Thr Val Gly Gly Thr 1 5 <210> 1156 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1156 Leu Asn Thr Val Gly Gly Thr Gly 1 5 <210> 1157 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1157 Ser Leu Asn Thr Val Gly Gly Thr 1 5 <210> 1158 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1158 Thr Ser Leu Asn Thr Val Gly Gly 1 5 <210> 1159 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1159 Glu Val Ser Gly Phe Glu Ile Pro 1 5 <210> 1160 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1160 Arg Ile Thr Arg Ser Ile Leu Gln 1 5 <210> 1161 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1161 Val Thr Thr Val Ala Ser His Thr 1 5 <210> 1162 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1162 Lys Asn Pro Lys Phe Met Glu Thr 1 5 <210> 1163 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1163 Pro Ala Gln Gly Thr Pro Asp Val 1 5 <210> 1164 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1164 Gln Gly Thr Pro Asp Val Ser Ser 1 5 <210> 1165 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1165 Gln Leu Ile Lys Ala Ile Gln Leu 1 5 <210> 1166 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1166 Glu Gly Phe Gly His Leu Ser Pro 1 5 <210> 1167 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1167 Asn Arg Leu Thr Ile Gly Glu Gly 1 5 <210> 1168 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1168 Arg Ser Arg Arg Glu Pro Pro Pro 1 5 <210> 1169 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1169 Ser Arg Arg Glu Pro Pro Pro Arg 1 5 <210> 1170 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1170 Gly Ser Val Thr Ser Tyr Val Leu 1 5 <210> 1171 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1171 Ser Val Thr Ser Tyr Val Leu Thr 1 5 <210> 1172 <211> 5 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1172 Met Ser Glu Thr Ala 1 5 <210> 1173 <211> 5 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1173 Met Ser Glu Thr Ala 1 5 <210> 1174 <211> 5 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1174 Met Ser Glu Thr Ala 1 5 <210> 1175 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1175 Cys Asn His Phe Thr His Phe Gly 1 5 <210> 1176 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1176 Cys Asn His Phe Thr His Phe Gly 1 5 <210> 1177 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1177 Ser Glu Ala Ser Tyr Glu Leu Thr 1 5 <210> 1178 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1178 Gly Ser Val Ala Ser Tyr Glu Leu 1 5 <210> 1179 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1179 Ser Trp Ala Gln Ser Val Leu Thr 1 5 <210> 1180 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1180 Gln Ser Val Leu Thr Gln Pro Pro 1 5 <210> 1181 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1181 Gly Ser Trp Ala Gln Ser Val Leu 1 5 <210> 1182 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1182 Ser Trp Ala Gln Ser Val Leu Thr 1 5 <210> 1183 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1183 Ser Tyr Glu Leu Thr Gln Pro Pro 1 5 <210> 1184 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1184 Gly Ser Val Ala Thr Pro Leu Gly 1 5 <210> 1185 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1185 Asp Thr Thr Gly Glu Ile Val Leu 1 5 <210> 1186 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1186 Thr Thr Gly Glu Ile Val Leu Thr 1 5 <210> 1187 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1187 Gly Ser Ser Gly Asp Val Val Met 1 5 <210> 1188 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1188 Gly Ser Ser Gly Asp Val Val Met 1 5 <210> 1189 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1189 Pro Val Gly Lys Phe Phe Gln Tyr 1 5 <210> 1190 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1190 Pro Val Gly Lys Phe Phe Gln Tyr 1 5 <210> 1191 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1191 Val Asn Phe Leu Ser Tyr Phe Val 1 5 <210> 1192 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1192 Ile Lys Lys Ala Gly Thr Glu Leu 1 5 <210> 1193 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1193 Phe Gln Thr Val Thr Asp Tyr Gly 1 5 <210> 1194 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1194 Gly Ser Ser Gly Asp Ile Val Met 1 5 <210> 1195 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1195 Gly Ser Ser Gly Asp Ile Val Met 1 5 <210> 1196 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1196 Arg Thr Ala Thr Ser Glu Tyr Gln 1 5 <210> 1197 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1197 Thr Ala Thr Ser Glu Tyr Gln Thr 1 5 <210> 1198 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1198 Leu Val His Ser Gln His Val Phe 1 5 <210> 1199 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1199 Ser Ala Glu Cys Thr Val Phe Leu 1 5 <210> 1200 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1200 Glu Cys Thr Val Phe Leu Asp His 1 5 <210> 1201 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1201 Gly Val Arg Ala Glu Glu Ala Gly 1 5 <210> 1202 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1202 Gly Val Arg Ala Glu Glu Ala Gly 1 5 <210> 1203 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1203 Arg Ser Lys Arg Asp Val Gly Ser 1 5 <210> 1204 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1204 Gly Glu Leu Arg Ile Glu Thr Lys 1 5 <210> 1205 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1205 Leu Val His Gly Glu Leu Arg Ile 1 5 <210> 1206 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1206 Asn His Met Ala Ala Gln Pro Gln 1 5 <210> 1207 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1207 His Ala Asn His Met Ala Ala Gln 1 5 <210> 1208 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1208 Gly Ala Val Thr Val Ala Trp Lys 1 5 <210> 1209 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1209 Gly Ala Val Thr Val Ala Trp Lys 1 5 <210> 1210 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1210 Ser Pro Val Lys Ala Gly Val Glu 1 5 <210> 1211 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1211 Lys Thr Trp Gly Gln Glu Gln Thr 1 5 <210> 1212 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1212 Asn Lys Val Asp Leu Ser Phe Ser 1 5 <210> 1213 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1213 Pro Thr Asp Ala Ser Val Ser Gly 1 5 <210> 1214 <211> 5 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1214 Met Ala Gln Gln Ala 1 5 <210> 1215 <211> 5 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1215 Met Thr Gly Leu Ser 1 5 <210> 1216 <211> 5 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1216 Met Thr Gly Leu Ser 1 5 <210> 1217 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1217 Gly Ser Ser Gly Asp Ile Val Met 1 5 <210> 1218 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1218 Gly Ser Ser Gly Asp Ile Val Met 1 5 <210> 1219 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1219 Arg Met Arg Arg Gly Ala Gly Gly 1 5 <210> 1220 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1220 Ser Asp Ala Phe His Asp Asn Leu 1 5 <210> 1221 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1221 Gly Asp Arg Asn Lys Pro Gly Val 1 5 <210> 1222 <211> 5 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1222 Met Ser Glu Thr Ser 1 5 <210> 1223 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1223 Lys Thr Arg Arg Glu Ala Glu Asp 1 5 <210> 1224 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1224 Gly Lys Phe Lys Ser Gly Phe Pro 1 5 <210> 1225 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1225 Asp Thr Thr Gly Glu Ile Val Leu 1 5 <210> 1226 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1226 Gly Ala Arg Cys Asp Ile Gln Met 1 5 <210> 1227 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1227 Ala Gly Phe Asp Phe Ser Phe Leu 1 5 <210> 1228 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1228 Cys Val Gly Ser Gln Glu Glu Ala 1 5 <210> 1229 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1229 Ala Gly His Ala Gln Arg Asp Pro 1 5 <210> 1230 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1230 Ala Gly His Ala Gln Arg Asp Pro 1 5 <210> 1231 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1231 Arg Asp Arg Arg Gln Ile Phe Leu 1 5 <210> 1232 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1232 Leu Leu Tyr Lys Ile Val Arg Gly 1 5 <210> 1233 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1233 Gly Ser Trp Ala Asn Phe Met Leu 1 5 <210> 1234 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1234 Ser Trp Ala Asn Phe Met Leu Thr 1 5 <210> 1235 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1235 Asp Thr Thr Gly Glu Ile Val Met 1 5 <210> 1236 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1236 Pro Thr Arg Gly Ser Val Leu Leu 1 5 <210> 1237 <211> 5 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1237 Met Ser Glu Thr Ala 1 5 <210> 1238 <211> 5 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1238 Met Thr Glu Lys Ala 1 5 <210> 1239 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1239 Phe Ala Arg Arg Glu Ala Pro Tyr 1 5 <210> 1240 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1240 Pro Trp Arg Ala Asp Asp Ile Leu 1 5 <210> 1241 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1241 Gly Ser Trp Ala Gln Ser Ala Leu 1 5 <210> 1242 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1242 Gln Ser Ala Leu Thr Gln Pro Pro 1 5 <210> 1243 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1243 Ser Ser Leu Ala Gln Pro Leu Val 1 5 <210> 1244 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1244 Thr Val Leu Gln Gln Gln Tyr Asn 1 5 <210> 1245 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1245 Leu Arg Asp Pro Ala Asp Ala Ser 1 5 <210> 1246 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1246 Gln Ala Gln Ala Glu Pro Leu Gln 1 5 <210> 1247 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1247 Leu Tyr Asp Asn Gln Glu Phe Pro 1 5 <210> 1248 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1248 Val Gly Leu Gly Glu Lys Lys Glu 1 5 <210> 1249 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1249 Gly Val Gln Cys Glu Val Gln Leu 1 5 <210> 1250 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1250 Ser Trp Ala Gln Ser Ala Leu Thr 1 5 <210> 1251 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1251 Asp Ile Asp Cys Lys Leu Met Pro 1 5 <210> 1252 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1252 Glu Gln Gly Arg Asp Gly Pro Pro 1 5 <210> 1253 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1253 Ser Leu Met Lys Arg Pro Pro Gly 1 5 <210> 1254 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1254 Ala Ile Arg His Phe Glu Asn Lys 1 5 <210> 1255 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1255 Gln Pro Ala His Leu Thr Phe Pro 1 5 <210> 1256 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1256 Arg His Arg Ala Arg His Lys Ala 1 5 <210> 1257 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1257 Ser Val Ala Ser Tyr Glu Leu Thr 1 5 <210> 1258 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1258 Pro Gly Gly Leu Gln Pro Leu Ser 1 5 <210> 1259 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1259 Arg Gln Val Arg Thr Ile Val Glu 1 5 <210> 1260 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1260 Met Asn Thr Phe Ser Val Val Pro 1 5 <210> 1261 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1261 Pro Gly Leu Arg Ala Ala Pro Gly 1 5 <210> 1262 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1262 Gly Ala Tyr Gly Asp Ile Val Met 1 5 <210> 1263 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1263 Arg Ala Gly Gly Ser Ile Pro Ile 1 5 <210> 1264 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1264 Lys Lys Pro Ser Gln Ser Ala Thr 1 5 <210> 1265 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1265 Val Ala Leu Pro Thr Val Ser Pro 1 5 <210> 1266 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1266 Asn Lys Pro Cys Ser Lys Gln Pro 1 5 <210> 1267 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1267 Gly Leu Asp Lys Val Pro Lys Asp 1 5 <210> 1268 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1268 His Pro Val Glu Leu Leu Ala Arg 1 5 <210> 1269 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1269 Leu Gly Tyr Pro Ile Lys Ala Pro 1 5 <210> 1270 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1270 Pro Gly Val Val Gly Val Pro Gly 1 5 <210> 1271 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1271 Gly Val Arg Gly Leu Thr Gly Pro 1 5 <210> 1272 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1272 Ser Asp Gly Leu Pro Gly Leu Lys 1 5 <210> 1273 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1273 Gln Ala Lys Asn Ile Ser Gln Asp 1 5 <210> 1274 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1274 Pro Gly Val Arg Leu Leu Gln Asp 1 5 <210> 1275 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1275 Gln Gly Leu Gln Gly Leu Pro Gly 1 5 <210> 1276 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1276 Asp Pro Gly Glu Ile Leu Gly His 1 5 <210> 1277 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1277 Pro Pro Gly Pro Pro Gly Asp Ile 1 5 <210> 1278 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1278 Gly Arg Leu Val Asp Thr Gly Pro 1 5 <210> 1279 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1279 Ala Asp Ser Gly Glu Gly Asp Phe 1 5 <210> 1280 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1280 Ala Trp Thr Ala Asp Ser Gly Glu 1 5 <210> 1281 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1281 Ser Pro Glu Ala Gln Ala Ala Ala 1 5 <210> 1282 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1282 Asp Met Ser Arg Lys Ala Phe Val 1 5 <210> 1283 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1283 Gly Pro Gly Gly Val Ala Ala Ala 1 5 <210> 1284 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1284 Gly Ala Lys Gly Tyr Arg Gly Pro 1 5 <210> 1285 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1285 Gly Pro Ser Gly His Met Gly Arg 1 5 <210> 1286 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1286 Ser Thr Gly Arg Asn Gly Phe Lys 1 5 <210> 1287 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1287 Leu Pro Ser Arg Ser Ser Lys Ile 1 5 <210> 1288 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1288 Phe Glu Ser Lys Ser Tyr Lys Met 1 5 <210> 1289 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1289 His Glu Arg Glu His Ile Leu Gly 1 5 <210> 1290 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1290 Gly Asn Arg Gly Pro Arg Gly Glu 1 5 <210> 1291 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1291 Phe Ser Pro Phe Arg Ser Ser Arg 1 5 <210> 1292 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1292 Leu Asn Asn Arg Gln Ile Arg Gly 1 5 <210> 1293 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1293 Ser Pro Phe Arg Ser Ser Arg Ile 1 5 <210> 1294 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1294 Ser Leu Leu Arg Ser Glu Glu Thr 1 5 <210> 1295 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1295 Trp Glu Ser Ala Ser Leu Leu Arg 1 5 <210> 1296 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1296 Arg Gln Ile Arg Gly Leu Glu Glu 1 5 <210> 1297 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1297 Ser Leu Leu Arg Ser Glu Glu Thr 1 5 <210> 1298 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1298 Arg Gln Ile Arg Gly Leu Glu Glu 1 5 <210> 1299 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1299 Trp Glu Ser Ala Ser Leu Leu Arg 1 5 <210> 1300 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1300 Thr Ser Gly Pro Asn Gln Glu Gln 1 5 <210> 1301 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1301 Glu Lys Gln Arg Lys His Asn Leu 1 5 <210> 1302 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1302 Ser Leu Leu Arg Ser Glu Glu Thr 1 5 <210> 1303 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1303 Trp Glu Ser Ala Ser Leu Leu Arg 1 5 <210> 1304 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1304 Leu Gly Ser Lys Ile Asn Val Lys 1 5 <210> 1305 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1305 Arg Gln Ile Arg Gly Leu Glu Glu 1 5 <210> 1306 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1306 Trp Glu Ser Ala Ser Leu Leu Arg 1 5 <210> 1307 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1307 Leu Asn Asn Arg Gln Ile Arg Gly 1 5 <210> 1308 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1308 Ser Arg Ile Val Arg Ser Leu Met 1 5 <210> 1309 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1309 Glu Ser Lys Ser Tyr Lys Met Ala 1 5 <210> 1310 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1310 Ser Lys Ser Tyr Lys Met Ala Asp 1 5 <210> 1311 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1311 Pro Ser Arg Gly Lys Ser Ser Ser 1 5 <210> 1312 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1312 Ser Tyr Lys Met Ala Asp Glu Ala 1 5 <210> 1313 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1313 Gly Gly Val Arg Gly Pro Arg Val 1 5 <210> 1314 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1314 Gly Gly Val Arg Gly Pro Arg Val 1 5 <210> 1315 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1315 Gly Gly Gly Val Arg Gly Pro Arg 1 5 <210> 1316 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1316 Ala Asn Asn Arg Asp Asn Thr Tyr 1 5 <210> 1317 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1317 Tyr Lys Met Ala Asp Glu Ala Gly 1 5 <210> 1318 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1318 Gly Gly Gly Val Arg Gly Pro Arg 1 5 <210> 1319 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1319 Met Arg Met Glu Leu Glu Arg Pro 1 5 <210> 1320 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1320 Gly Gly Val Arg Gly Pro Arg Val 1 5 <210> 1321 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1321 Ser Ser Gly Pro Gly Ser Thr Gly 1 5 <210> 1322 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1322 Gly Gly Val Arg Gly Pro Arg Val 1 5 <210> 1323 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1323 Tyr Lys Met Ala Asp Glu Ala Gly 1 5 <210> 1324 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1324 Thr Phe Glu Ser Lys Ser Tyr Lys 1 5 <210> 1325 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1325 Pro Arg Val Val Glu Arg His Gln 1 5 <210> 1326 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1326 Pro Glu Trp Lys Ala Leu Thr Asp 1 5 <210> 1327 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1327 Gly Asn Phe Lys Ser Gln Leu Gln 1 5 <210> 1328 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1328 Gly Gly Val Arg Gly Pro Arg Val 1 5 <210> 1329 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1329 Gly Pro Arg Val Val Glu Arg His 1 5 <210> 1330 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1330 Pro Ser Arg Gly Lys Ser Ser Ser 1 5 <210> 1331 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1331 Gly Asn Phe Lys Ser Gln Leu Gln 1 5 <210> 1332 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1332 Ser Gln Leu Gln Lys Val Pro Pro 1 5 <210> 1333 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1333 Ser Ser Gly Pro Gly Ser Thr Gly 1 5 <210> 1334 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1334 Met Arg Met Glu Leu Glu Arg Pro 1 5 <210> 1335 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1335 Pro Ser Arg Gly Lys Ser Ser Ser 1 5 <210> 1336 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1336 Pro Arg Val Val Glu Arg His Gln 1 5 <210> 1337 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1337 Ser Ala Asn Asn Arg Asp Asn Thr 1 5 <210> 1338 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1338 Arg Val Val Glu Arg His Gln Ser 1 5 <210> 1339 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1339 Lys Ala Leu Thr Asp Met Pro Gln 1 5 <210> 1340 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1340 Trp Gly Thr Phe Glu Glu Val Ser 1 5 <210> 1341 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1341 Pro Gly Asn Phe Lys Ser Gln Leu 1 5 <210> 1342 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1342 Ser Pro Arg Asn Pro Ser Ser Ala 1 5 <210> 1343 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1343 Pro Gly Asn Phe Lys Ser Gln Leu 1 5 <210> 1344 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1344 Pro Gln Met Arg Met Glu Leu Glu 1 5 <210> 1345 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1345 Glu Arg His Gln Ser Ala Cys Lys 1 5 <210> 1346 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1346 Lys Ala Leu Thr Asp Met Pro Gln 1 5 <210> 1347 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1347 Thr Phe Glu Ser Lys Ser Tyr Lys 1 5 <210> 1348 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1348 Pro Ser Arg Gly Lys Ser Ser Ser 1 5 <210> 1349 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1349 Gly Asn Arg Asn Pro Gly Ser Ser 1 5 <210> 1350 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1350 Ser Lys Ser Tyr Lys Met Ala Asp 1 5 <210> 1351 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1351 Trp Gly Thr Phe Glu Glu Val Ser 1 5 <210> 1352 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1352 Pro Ser Arg Gly Lys Ser Ser Ser 1 5 <210> 1353 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1353 Met Glu Leu Glu Arg Pro Gly Gly 1 5 <210> 1354 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1354 Leu Val Thr Ser Lys Gly Asp Lys 1 5 <210> 1355 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1355 Gly Ser Trp Asn Ser Gly Ser Ser 1 5 <210> 1356 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1356 Thr Phe Pro Gly Phe Phe Ser Pro 1 5 <210> 1357 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1357 Arg Gly His Ala Lys Ser Arg Pro 1 5 <210> 1358 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1358 Pro Gly Asn Phe Lys Ser Gln Leu 1 5 <210> 1359 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1359 Leu Ala His Gln Ser Asn Ser Thr 1 5 <210> 1360 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1360 Leu Ala His Gln Ser Asn Ser Thr 1 5 <210> 1361 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1361 Ala His Gln Ser Asn Ser Thr Asn 1 5 <210> 1362 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1362 Ala His Gln Ser Asn Ser Thr Asn 1 5 <210> 1363 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1363 Gln Leu Ala His Gln Ser Asn Ser 1 5 <210> 1364 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1364 Gln Leu Ala His Gln Ser Asn Ser 1 5 <210> 1365 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1365 Arg Gln Leu Ala His Gln Ser Asn 1 5 <210> 1366 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1366 Leu Ala His Gln Ser Asn Ser Thr 1 5 <210> 1367 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1367 Gln Val Val Lys Gly Ser Val Phe 1 5 <210> 1368 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1368 Val Pro Arg Gly Gln Val Val Lys 1 5 <210> 1369 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1369 Pro Ser Arg Asn Asn Val Pro Cys 1 5 <210> 1370 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1370 Ser Arg Asn Asn Val Pro Cys Ser 1 5 <210> 1371 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1371 Val Pro Leu Ser Val Gly Val Gln 1 5 <210> 1372 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1372 Gly Ser Val Phe Leu Arg Asn Pro 1 5 <210> 1373 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1373 Val Gln Leu Gln Asp Val Pro Arg 1 5 <210> 1374 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1374 Val Gly Val Gln Leu Gln Asp Val 1 5 <210> 1375 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1375 Asn Arg Gln Ile Arg Gly Leu Glu 1 5 <210> 1376 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1376 Val His Leu Gly Val Pro Leu Ser 1 5 <210> 1377 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1377 Arg Gln Ile Arg Gly Leu Glu Glu 1 5 <210> 1378 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1378 Gly Arg Arg Asn Arg Arg Arg Arg 1 5 <210> 1379 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1379 Ser Val Val His Leu Gly Val Pro 1 5 <210> 1380 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1380 Ile Asn Val Lys Val Gly Gly Asn 1 5 <210> 1381 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1381 Pro Val Thr Pro Leu Gln Leu Phe 1 5 <210> 1382 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1382 Pro Val Thr Pro Leu Gln Leu Phe 1 5 <210> 1383 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1383 Asn Arg Gln Ile Arg Gly Leu Glu 1 5 <210> 1384 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1384 Thr Pro Leu Gln Leu Phe Glu Gly 1 5 <210> 1385 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1385 Val Phe Leu Arg Asn Pro Ser Arg 1 5 <210> 1386 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1386 Pro Leu Gln Leu Phe Glu Gly Arg 1 5 <210> 1387 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1387 Leu Gly Ser Lys Ile Asn Val Lys 1 5 <210> 1388 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1388 Val Arg Val Thr Ala Ser Asp Pro 1 5 <210> 1389 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1389 Val Gly Val Gln Leu Gln Asp Val 1 5 <210> 1390 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1390 Ala Arg Leu Thr Val Ala Ala Pro 1 5 <210> 1391 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1391 Pro Arg Val Gly Asp Thr Leu Asn 1 5 <210> 1392 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1392 Val Pro Leu Ser Val Gly Val Gln 1 5 <210> 1393 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1393 Gly Arg Arg Asn Arg Arg Arg Arg 1 5 <210> 1394 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1394 Gly Arg Arg Asn Arg Arg Arg Arg 1 5 <210> 1395 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1395 Val Pro Leu Ser Val Gly Val Gln 1 5 <210> 1396 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1396 Gly Arg Arg Asn Arg Arg Arg Arg 1 5 <210> 1397 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1397 Gln Val Val Lys Gly Ser Val Phe 1 5 <210> 1398 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1398 Val His Leu Gly Val Pro Leu Ser 1 5 <210> 1399 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1399 Pro Arg Val Gly Asp Thr Leu Asn 1 5 <210> 1400 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1400 Gly Gly Gly Tyr Arg Ala Arg Pro 1 5 <210> 1401 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1401 Gly Gly Gly Tyr Arg Ala Arg Pro 1 5 <210> 1402 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1402 Gly Gly Gly Tyr Arg Ala Arg Pro 1 5 <210> 1403 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1403 Gly Gly Gly Tyr Arg Ala Arg Pro 1 5 <210> 1404 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1404 Phe Ser Ala Arg Gly His Arg Pro 1 5 <210> 1405 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1405 Ala Arg Gly His Arg Pro Leu Asp 1 5 <210> 1406 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1406 Phe Phe Ser Ala Arg Gly His Arg 1 5 <210> 1407 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1407 Lys Lys Arg Glu Glu Ala Pro Ser 1 5 <210> 1408 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1408 Gly Gly Gly Tyr Arg Ala Arg Pro 1 5 <210> 1409 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1409 Gly Gly Tyr Arg Ala Arg Pro Ala 1 5 <210> 1410 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1410 Arg Pro Leu Asp Lys Lys Arg Glu 1 5 <210> 1411 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1411 Gly Gly Gly Tyr Arg Ala Arg Pro 1 5 <210> 1412 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1412 Asp Lys Lys Arg Glu Glu Ala Pro 1 5 <210> 1413 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1413 Phe Phe Ser Ala Arg Gly His Arg 1 5 <210> 1414 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1414 Arg Pro Ala Lys Ala Ala Ala Thr 1 5 <210> 1415 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1415 Gly Phe Phe Ser Ala Arg Gly His 1 5 <210> 1416 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1416 Arg Pro Leu Asp Lys Lys Arg Glu 1 5 <210> 1417 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1417 Gly Gly Tyr Arg Ala Arg Pro Ala 1 5 <210> 1418 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1418 Pro Leu Asp Lys Lys Arg Glu Glu 1 5 <210> 1419 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1419 Ala Pro Ser Leu Arg Pro Ala Pro 1 5 <210> 1420 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1420 Glu Ala Pro Ser Leu Arg Pro Ala 1 5 <210> 1421 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1421 Leu Asp Lys Lys Arg Glu Glu Ala 1 5 <210> 1422 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1422 Phe Phe Ser Ala Arg Gly His Arg 1 5 <210> 1423 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1423 Gly Gly Tyr Arg Ala Arg Pro Ala 1 5 <210> 1424 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1424 Gly Gly Gly Tyr Arg Ala Arg Pro 1 5 <210> 1425 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1425 Arg Pro Leu Asp Lys Lys Arg Glu 1 5 <210> 1426 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1426 Arg Ala Arg Pro Ala Lys Ala Ala 1 5 <210> 1427 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1427 Ala Lys Ala Ala Ala Thr Gln Lys 1 5 <210> 1428 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1428 Phe Phe Ser Ala Arg Gly His Arg 1 5 <210> 1429 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1429 Pro Pro Ile Ser Gly Gly Gly Tyr 1 5 <210> 1430 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1430 Lys Arg Glu Glu Ala Pro Ser Leu 1 5 <210> 1431 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1431 Ala Arg Pro Ala Lys Ala Ala Ala 1 5 <210> 1432 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1432 Glu Ala Phe Asp Gly Ala Arg Asp 1 5 <210> 1433 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1433 Lys Arg Gly Pro Gly Gly Val Trp 1 5 <210> 1434 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1434 Lys Arg Gly Pro Gly Gly Val Trp 1 5 <210> 1435 <211> 5 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1435 Leu Pro Glu Lys Tyr 1 5 <210> 1436 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1436 Lys Arg Gly Pro Gly Gly Val Trp 1 5 <210> 1437 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1437 Phe Arg Pro Ala Gly Leu Pro Glu 1 5 <210> 1438 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1438 Gly Ala Glu Asp Ser Leu Ala Asp 1 5 <210> 1439 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1439 Lys Arg Gly Pro Gly Gly Val Trp 1 5 <210> 1440 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1440 Phe Ser Phe Leu Gly Glu Ala Phe 1 5 <210> 1441 <211> 5 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1441 Thr Asn Pro Lys Glu 1 5 <210> 1442 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1442 Thr Ala Leu Lys Ser Pro Pro Gly 1 5 <210> 1443 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1443 Thr Leu Leu Lys Leu Gly Asn Gln 1 5 <210> 1444 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1444 Thr Ala Leu Lys Ser Pro Pro Gly 1 5 <210> 1445 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1445 Thr Leu Leu Lys Leu Gly Asn Gln 1 5 <210> 1446 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1446 Thr Ser Gly Pro Asn Gln Glu Gln 1 5 <210> 1447 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1447 Thr Ser Gly Pro Asn Gln Glu Gln 1 5 <210> 1448 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1448 Thr Leu Leu Lys Leu Gly Asn Gln 1 5 <210> 1449 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1449 Leu Lys Leu Gly Asn Gln Glu Pro 1 5 <210> 1450 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1450 Lys Glu Gln Gln Asp Ser Pro Gly 1 5 <210> 1451 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1451 Pro Leu Thr Leu Leu Lys Leu Gly 1 5 <210> 1452 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1452 Gly Lys Gln Leu Asn Leu Lys Leu 1 5 <210> 1453 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1453 Asp Val Leu Lys Asp Ser Gly Arg 1 5 <210> 1454 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1454 Arg Gln Glu Met Ser Lys Asp Leu 1 5 <210> 1455 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1455 Arg Val Lys Asp Leu Ala Thr Val 1 5 <210> 1456 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1456 His Glu Leu Gln Glu Lys Leu Ser 1 5 <210> 1457 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1457 Ser Pro Leu Gly Glu Glu Met Arg 1 5 <210> 1458 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1458 Ala Thr Val Tyr Val Asp Val Leu 1 5 <210> 1459 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1459 Glu Asn Leu Thr Gln Glu Asn Gln 1 5 <210> 1460 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1460 Leu Gly Leu Ala Ser Ala Asn Val 1 5 <210> 1461 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1461 Met Asn Glu Asp Lys Arg His Ser 1 5 <210> 1462 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1462 Gln Met Asn Glu Asp Lys Arg His 1 5 <210> 1463 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1463 Met Asn Glu Asp Lys Arg His Ser 1 5 <210> 1464 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1464 Met Asn Glu Asp Lys Arg His Ser 1 5 <210> 1465 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1465 Arg Ala Gln Asp Phe Val Gln Trp 1 5 <210> 1466 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1466 Gln Met Asn Glu Asp Lys Arg His 1 5 <210> 1467 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1467 Leu Met Asn Thr Lys Arg Asn Arg 1 5 <210> 1468 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1468 Met Asn Glu Asp Lys Arg His Ser 1 5 <210> 1469 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1469 Gln Met Asn Glu Asp Lys Arg His 1 5 <210> 1470 <211> 6 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1470 Lys Ile Thr Asp Arg Lys 1 5 <210> 1471 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1471 Lys Gly Arg Gly Arg Arg Asp Phe 1 5 <210> 1472 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1472 Pro Met Phe Gln Arg Arg Arg Arg 1 5 <210> 1473 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1473 Trp Met Pro Met Phe Gln Arg Arg 1 5 <210> 1474 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1474 Ser Trp Met Pro Met Phe Gln Arg 1 5 <210> 1475 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1475 Gly Ala Arg Ala Ser Trp Met Pro 1 5 <210> 1476 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1476 Ala Arg Ala Ser Trp Met Pro Met 1 5 <210> 1477 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1477 Arg Ala Gly Ala Arg Ala Ser Trp 1 5 <210> 1478 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1478 Ala Arg Ala Ser Trp Met Pro Met 1 5 <210> 1479 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1479 Ala Arg Ala Ser Trp Met Pro Met 1 5 <210> 1480 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1480 Arg Ala Gly Ala Arg Ala Ser Trp 1 5 <210> 1481 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1481 Gln Leu Ala Glu Leu Gln Pro Gln 1 5 <210> 1482 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1482 Ala Gly Ala Arg Ala Ser Trp Met 1 5 <210> 1483 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1483 Glu Leu Gln Pro Gln Asp Arg Ala 1 5 <210> 1484 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1484 Asp Pro Asn His Phe Arg Pro Ala 1 5 <210> 1485 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1485 Asp Pro Asn His Phe Arg Pro Ala 1 5 <210> 1486 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1486 Asp Pro Asn His Phe Arg Pro Ala 1 5 <210> 1487 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1487 Ala Glu Val Ile Ser Asn Ala Arg 1 5 <210> 1488 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1488 Lys Ser Lys Leu Lys Lys Thr Glu 1 5 <210> 1489 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1489 Lys Lys Thr Glu Thr Gln Glu Lys 1 5 <210> 1490 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1490 Glu Thr Gln Glu Lys Asn Pro Leu 1 5 <210> 1491 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1491 Met Val Ser His His Asn Leu Thr 1 5 <210> 1492 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1492 Val Ser His His Asn Leu Thr Thr 1 5 <210> 1493 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1493 Ala Lys Met Val Ser His His Asn 1 5 <210> 1494 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1494 Phe Pro Trp Gln Ala Lys Met Val 1 5 <210> 1495 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1495 Leu Trp Gly Gln Leu Phe Ala Val 1 5 <210> 1496 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1496 Leu Trp Gly Gln Leu Phe Ala Val 1 5 <210> 1497 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1497 Leu Glu Arg Met Phe Leu Ser Phe 1 5 <210> 1498 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1498 Glu Arg Met Phe Leu Ser Phe Pro 1 5 <210> 1499 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1499 Phe Leu Ser Phe Pro Thr Thr Lys 1 5 <210> 1500 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1500 Gly Lys Val Gly Ala His Ala Gly 1 5 <210> 1501 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1501 Ser Asp Met Arg Gln Glu Lys Pro 1 5 <210> 1502 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1502 Gln His Pro Gly Ser Asp Met Arg 1 5 <210> 1503 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1503 Gly Ser Asp Met Arg Gln Glu Lys 1 5 <210> 1504 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1504 His Val Leu Leu Ala Ala Pro Pro 1 5 <210> 1505 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1505 Val Leu Leu Ala Ala Pro Pro Gly 1 5 <210> 1506 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1506 Pro Arg Lys Thr Arg Thr Val Val 1 5 <210> 1507 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1507 Pro Arg Lys Thr Arg Thr Val Val 1 5 <210> 1508 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1508 Pro Arg Lys Thr Arg Thr Val Val 1 5 <210> 1509 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1509 Ser His Val Leu Leu Ala Ala Pro 1 5 <210> 1510 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1510 Ser His Pro Arg Lys Thr Arg Thr 1 5 <210> 1511 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1511 Lys Asp Val Met Glu Lys Arg Glu 1 5 <210> 1512 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1512 Asp Val Met Glu Lys Arg Glu Asp 1 5 <210> 1513 <211> 5 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1513 Ala Leu Arg Arg Gly 1 5 <210> 1514 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1514 Lys Asp Val Met Glu Lys Arg Glu 1 5 <210> 1515 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1515 Gly Pro Gln Leu Arg Arg Gly Trp 1 5 <210> 1516 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1516 Lys Leu Ser Phe Arg Ala Arg Ala 1 5 <210> 1517 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1517 Ser Leu Leu Arg Ser Glu Glu Thr 1 5 <210> 1518 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1518 Ala Ser Leu Leu Arg Ser Glu Glu 1 5 <210> 1519 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1519 Ala Ser Leu Leu Arg Ser Glu Glu 1 5 <210> 1520 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1520 Ala Ser Leu Leu Arg Ser Glu Glu 1 5 <210> 1521 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1521 His Asp Ala Gln Gly Asp Val Pro 1 5 <210> 1522 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1522 Ala Ser Leu Leu Arg Ser Glu Glu 1 5 <210> 1523 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1523 Ala Ser Leu Leu Arg Ser Glu Glu 1 5 <210> 1524 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1524 Ala Ser Leu Leu Arg Ser Glu Glu 1 5 <210> 1525 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1525 Ala Ser Leu Leu Arg Ser Glu Glu 1 5 <210> 1526 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1526 Pro Ser Leu Ala Lys Lys Gln Arg 1 5 <210> 1527 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1527 Ile Tyr Ile Ser Gly Met Ala Pro 1 5 <210> 1528 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1528 Lys Pro Glu Gly Ile Asp Ser Arg 1 5 <210> 1529 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1529 Pro Ser Leu Ala Lys Lys Gln Arg 1 5 <210> 1530 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1530 Ala Pro Arg Pro Ser Leu Ala Lys 1 5 <210> 1531 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1531 Pro Ser Leu Ala Lys Lys Gln Arg 1 5 <210> 1532 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1532 Pro Arg Pro Ser Leu Ala Lys Lys 1 5 <210> 1533 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1533 Lys Leu Leu Gln Asp Glu Phe Pro 1 5 <210> 1534 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1534 Pro Pro Glu Lys Lys Glu Lys Gly 1 5 <210> 1535 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1535 Glu Lys Lys Glu Lys Gly Tyr Pro 1 5 <210> 1536 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1536 Gln Gly His Asn Ser Val Phe Leu 1 5 <210> 1537 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1537 Tyr Pro Pro Glu Lys Lys Glu Lys 1 5 <210> 1538 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1538 Lys Leu Leu Gln Asp Glu Phe Pro 1 5 <210> 1539 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1539 Gln Ser Gln Thr Gln Pro Val Ser 1 5 <210> 1540 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1540 Pro Val Ala Ser Lys Phe Ser Pro 1 5 <210> 1541 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1541 Leu His Val Gln Ser Gln Thr Gln 1 5 <210> 1542 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1542 Ala Pro Ala Phe Tyr Ala Pro Gln 1 5 <210> 1543 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1543 Gln Pro Val Ser Leu Ala Asn Thr 1 5 <210> 1544 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1544 Gln Arg Ala Gln Met Gly Arg Val 1 5 <210> 1545 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1545 Thr Ala Lys Asp Ala Leu Ser Ser 1 5 <210> 1546 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1546 Thr Lys Thr Ala Lys Asp Ala Leu 1 5 <210> 1547 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1547 Ala Gln Gln Ala Arg Gly Trp Val 1 5 <210> 1548 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1548 Glu His Ile Ala Lys Arg Ala Met 1 5 <210> 1549 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1549 Glu His Ile Ala Lys Arg Ala Met 1 5 <210> 1550 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1550 Gly Arg Glu His Ile Ala Lys Arg 1 5 <210> 1551 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1551 Ala Pro Val Ser Lys Arg Phe Pro 1 5 <210> 1552 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1552 Ala Pro Val Ser Lys Arg Phe Pro 1 5 <210> 1553 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1553 Asp Gly Leu Ser Val Glu Asp Ile 1 5 <210> 1554 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1554 Pro Met Tyr Glu Glu Asn Ser Arg 1 5 <210> 1555 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1555 Val Ser Leu Lys Ala Pro Leu Thr 1 5 <210> 1556 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1556 Ala Pro Leu Thr Lys Pro Leu Lys 1 5 <210> 1557 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1557 Ser Tyr Val Ser Leu Lys Ala Pro 1 5 <210> 1558 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1558 Gln Tyr Leu Gln Gln Cys Pro Phe 1 5 <210> 1559 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1559 Glu Asn Phe Lys Ala Leu Val Leu 1 5 <210> 1560 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1560 Ala Leu Val Leu Ile Ala Phe Ala 1 5 <210> 1561 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1561 Ala Val Pro Arg Glu Leu Ser Pro 1 5 <210> 1562 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1562 Leu Arg Arg Tyr Ile Asn Met Leu 1 5 <210> 1563 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1563 Arg Pro Arg Tyr Gly Lys Arg His 1 5 <210> 1564 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1564 Arg Pro Arg Tyr Gly Lys Arg His 1 5 <210> 1565 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1565 Val Arg Gly Ala Arg Asn Ser Glu 1 5 <210> 1566 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1566 Ala Pro Glu Val Arg Gly Ala Arg 1 5 <210> 1567 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1567 Val Arg Gly Ala Arg Asn Ser Glu 1 5 <210> 1568 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1568 Pro Thr His Val Arg Ser Pro Gln 1 5 <210> 1569 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1569 Pro Thr His Val Arg Ser Pro Gln 1 5 <210> 1570 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1570 Ala Pro Glu Val Arg Gly Ala Arg 1 5 <210> 1571 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1571 Leu Thr Glu Thr Val Arg Ser Gln 1 5 <210> 1572 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1572 Glu Leu Pro Asp Trp Asn Glu Val 1 5 <210> 1573 <211> 6 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1573 Glu Asp Thr Lys Ser Gly 1 5 <210> 1574 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1574 Trp Asp Tyr Ala Ser Asp His Gly 1 5 <210> 1575 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1575 Thr Asn Gln Tyr Asn Asn Pro Ala 1 5 <210> 1576 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1576 Ala Pro Val Thr Lys Val Ala Ala 1 5 <210> 1577 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1577 Ser Gly Val Glu Ala Asn Ser Arg 1 5 <210> 1578 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1578 Tyr His Glu Gln Leu Ser Val Ala 1 5 <210> 1579 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1579 His Glu Gln Leu Ser Val Ala Glu 1 5 <210> 1580 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1580 Glu Ile Thr Asn Ala Cys Phe Glu 1 5 <210> 1581 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1581 Leu Gly Arg Leu Leu Val Val Tyr 1 5 <210> 1582 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1582 Thr Gln Arg Phe Phe Glu Ser Phe 1 5 <210> 1583 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1583 Thr Gln Arg Phe Phe Glu Ser Phe 1 5 <210> 1584 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1584 Arg Ala Pro Arg Glu Thr Tyr Leu 1 5 <210> 1585 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1585 Arg Ala Pro Arg Glu Thr Tyr Leu 1 5 <210> 1586 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1586 Asn Arg Ala Pro Arg Glu Thr Tyr 1 5 <210> 1587 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1587 Arg Ala Pro Arg Glu Thr Tyr Leu 1 5 <210> 1588 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1588 Arg Arg Tyr Gln Arg Ser Leu Pro 1 5 <210> 1589 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1589 Arg Met Leu Ala Asp Ala Pro Pro 1 5 <210> 1590 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1590 Pro Val Glu Val Ser Arg Lys Asn 1 5 <210> 1591 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1591 Ala Thr Leu Lys Ser Arg Lys Met 1 5 <210> 1592 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1592 His Leu Ile Ser Thr Gln Ser Ala 1 5 <210> 1593 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1593 Pro Ser Val Ser Val Ala Pro Gly 1 5 <210> 1594 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1594 Pro Ser Val Ser Val Ala Pro Gly 1 5 <210> 1595 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1595 Lys Lys Lys Ala Arg Lys Ser Ala 1 5 <210> 1596 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1596 Lys Thr Pro Val Lys Lys Lys Ala 1 5 <210> 1597 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1597 Thr Pro Val Lys Lys Lys Ala Arg 1 5 <210> 1598 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1598 Arg Ser Ala Ser Gln Leu Asp Ala 1 5 <210> 1599 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1599 Gln Leu Asp Ala Arg Asn Thr Lys 1 5 <210> 1600 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1600 Pro Ser Val Ser Val Ser Pro Gly 1 5 <210> 1601 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1601 Pro Ser Val Ser Val Ser Pro Gly 1 5 <210> 1602 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1602 Pro Ser Val Ser Ala Ala Pro Gly 1 5 <210> 1603 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1603 Pro Ser Val Ser Ala Ala Pro Gly 1 5 <210> 1604 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1604 Pro Ser Val Ser Glu Ala Pro Arg 1 5 <210> 1605 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1605 Pro Ser Val Ser Glu Ala Pro Arg 1 5 <210> 1606 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1606 Pro Ser Val Ser Val Ser Pro Gly 1 5 <210> 1607 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1607 Gly Arg Leu Ala Ser Pro Gly Phe 1 5 <210> 1608 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1608 Gly Thr Leu Ser Leu Ser Pro Gly 1 5 <210> 1609 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1609 Gly Thr Leu Ser Leu Ser Pro Gly 1 5 <210> 1610 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1610 Leu Pro Val Thr Leu Gly Gln Pro 1 5 <210> 1611 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1611 Ser Pro Leu Ser Leu Pro Val Thr 1 5 <210> 1612 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1612 Gln Ser Thr Gln Arg Leu Arg Arg 1 5 <210> 1613 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1613 Thr Gln Arg Leu Arg Arg Gly Leu 1 5 <210> 1614 <211> 6 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1614 Thr Gln Pro Ala Thr Gln 1 5 <210> 1615 <211> 6 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1615 Thr Gln Pro Ala Thr Gln 1 5 <210> 1616 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1616 Ser Pro Glu Leu Gln Ala Glu Ala 1 5 <210> 1617 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1617 Ser Pro Val Thr Leu Gly Gln Pro 1 5 <210> 1618 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1618 Thr Pro Leu Ser Ser Pro Val Thr 1 5 <210> 1619 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1619 Phe Asn Pro Arg Thr Phe Gly Ser 1 5 <210> 1620 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1620 Phe Asn Pro Arg Thr Phe Gly Ser 1 5 <210> 1621 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1621 Leu Gln Arg Val Arg Arg Ala Asn 1 5 <210> 1622 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1622 Asn Arg Pro Lys Arg Tyr Asn Ser 1 5 <210> 1623 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1623 Asn Arg Pro Lys Arg Tyr Asn Ser 1 5 <210> 1624 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1624 Lys Pro Leu Gly Asp Trp Ala Ala 1 5 <210> 1625 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1625 Gln Ser Lys Pro Leu Gly Asp Trp 1 5 <210> 1626 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1626 Lys Arg Arg Gln Lys Arg Glu Trp 1 5 <210> 1627 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1627 Lys Arg Arg Gln Lys Arg Glu Trp 1 5 <210> 1628 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1628 Pro His Pro Phe Ala Val Val Pro 1 5 <210> 1629 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1629 Pro His Pro Phe Ala Val Val Pro 1 5 <210> 1630 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1630 Ala Gly Val Glu Thr Thr Thr Pro 1 5 <210> 1631 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1631 Ser Tyr Leu Ser Leu Thr Pro Glu 1 5 <210> 1632 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1632 Ser Tyr Leu Ser Leu Thr Pro Glu 1 5 <210> 1633 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1633 Phe Arg Val Gly Ala Ser Glu Asn 1 5 <210> 1634 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1634 Leu Arg Val Thr Ala Ala Pro Gln 1 5 <210> 1635 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1635 Ser Leu Leu His Thr Glu Thr Thr 1 5 <210> 1636 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1636 Asp Lys Asn Phe Ile Asn Asn Pro 1 5 <210> 1637 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1637 Asn Gly Gly Leu Ile Phe Ala Gly 1 5 <210> 1638 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1638 Asp Val Asp Pro Phe Tyr Tyr Asp 1 5 <210> 1639 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1639 Ser Pro Leu Ser Leu Pro Val Thr 1 5 <210> 1640 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1640 Leu Pro Val Thr Pro Gly Glu Pro 1 5 <210> 1641 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1641 Val Val Pro Arg Gly Val Asn Leu 1 5 <210> 1642 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1642 Gly Ser Leu Gln Lys Arg Gly Ile 1 5 <210> 1643 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1643 Ala Thr Leu Ser Leu Ser Pro Gly 1 5 <210> 1644 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1644 Ser Ser Leu Ser Ala Ser Val Gly 1 5 <210> 1645 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1645 Gln Pro Pro Gln Glu Lys Ala His 1 5 <210> 1646 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1646 Arg Val Pro Arg Gln Val Arg Leu 1 5 <210> 1647 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1647 Ala Ala Lys Val Tyr Ser Leu Phe 1 5 <210> 1648 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1648 Arg Pro Gly Gly Ser Tyr Pro Ala 1 5 <210> 1649 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1649 Gln Pro Ser Arg Leu Gln Asp Pro 1 5 <210> 1650 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1650 Leu Pro Arg Leu Lys Arg Arg Asp 1 5 <210> 1651 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1651 His Ser Val Ser Glu Ser Pro Gly 1 5 <210> 1652 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1652 His Ser Val Ser Glu Ser Pro Gly 1 5 <210> 1653 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1653 Ala Thr Leu Ser Val Ser Pro Gly 1 5 <210> 1654 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1654 Gln Gln Leu Thr Ser Pro Gly Tyr 1 5 <210> 1655 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1655 Lys Lys Ala Ala Lys Lys Ala Gly 1 5 <210> 1656 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1656 Lys Leu Asn Tyr Lys Pro Pro Pro 1 5 <210> 1657 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1657 Ser Arg Asp Thr Arg Arg Ser Phe 1 5 <210> 1658 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1658 His His Ser Ser Tyr Val His Leu 1 5 <210> 1659 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1659 Pro Ser Val Ser Gly Ser Pro Gly 1 5 <210> 1660 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1660 Pro Ser Val Ser Gly Ser Pro Gly 1 5 <210> 1661 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1661 Phe Gln Val Gly Ser Met Pro Pro 1 5 <210> 1662 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1662 His Ser Arg Glu Arg Ala Asp Glu 1 5 <210> 1663 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1663 Pro Glu Gln Ile Ala Ala Asp Ile 1 5 <210> 1664 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1664 Pro Glu Lys Phe Lys Pro Glu His 1 5 <210> 1665 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1665 Arg Gly Pro Arg Tyr Ala Glu Gly 1 5 <210> 1666 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1666 Gly Ser Leu Arg Leu Ser Cys Ala 1 5 <210> 1667 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1667 Arg Ser Val Ser Gly Ser Pro Gly 1 5 <210> 1668 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1668 Pro Pro Pro Pro Pro Gly Pro Met 1 5 <210> 1669 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1669 Pro Pro Gly Pro Lys Val Ser Val 1 5 <210> 1670 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1670 Phe Ser Pro Phe Arg Ser Ser Arg 1 5 <210> 1671 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1671 Ala Val Glu Thr Leu Ile Cys Ser 1 5 <210> 1672 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1672 Ala Asp Lys Glu Lys Glu Leu Arg 1 5 <210> 1673 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1673 Ser Ser Val Ser Val Ser Pro Gly 1 5 <210> 1674 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1674 Leu Ser Phe Gln Asn Pro Val Tyr 1 5 <210> 1675 <211> 5 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1675 His Gln Thr Thr Arg 1 5 <210> 1676 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1676 Glu Pro Tyr Asn Ala Thr Leu Ser 1 5 <210> 1677 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1677 Trp His Leu Ser Lys Arg Asp Thr 1 5 <210> 1678 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1678 Ser Leu Ala Val Ser Leu Gly Glu 1 5 <210> 1679 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1679 Gly Glu Val Thr Ser Pro Leu Phe 1 5 <210> 1680 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1680 Ser Pro Ser Pro Ala Ala Ser Ala 1 5 <210> 1681 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1681 Ser Pro Pro Gly Val Asp Ala Lys 1 5 <210> 1682 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1682 Thr Pro Ser Pro Ala Ala Pro Pro 1 5 <210> 1683 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1683 Gly Gly Val Arg Gly Pro Arg Val 1 5 <210> 1684 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1684 Gly Gly Val Arg Gly Pro Arg Val 1 5 <210> 1685 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1685 Arg Gln Ile Arg Gly Leu Glu Glu 1 5 <210> 1686 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1686 Ser Leu Leu Arg Ser Glu Glu Thr 1 5 <210> 1687 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1687 Arg Pro Val Arg Asp Cys Asp Asp 1 5 <210> 1688 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1688 Gly Gly Pro Gly Pro Gln Gly Pro Pro Gly 1 5 10 <210> 1689 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1689 Cys Gly Gln Pro Pro Val Val Glu Asn Ala 1 5 10 <210> 1690 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1690 Gly Pro Pro Gly Arg Asp Gly Ala Ala Gly 1 5 10 <210> 1691 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1691 Gln Pro Leu Gly Met Ile Ser Leu Met Lys 1 5 10 <210> 1692 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1692 Leu Ser Ser Thr Gly Arg Asn Gly Phe Lys 1 5 10 <210> 1693 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1693 Gln Pro Leu Gly Met Ile Ser Leu Met Lys 1 5 10 <210> 1694 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1694 Ser Arg Ser Ser Lys Ile Thr His Arg Ile 1 5 10 <210> 1695 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1695 Leu Gln Leu Pro Ser Arg Ser Ser Lys Ile 1 5 10 <210> 1696 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1696 Thr Gly Arg Asn Gly Phe Lys Ser His Ala 1 5 10 <210> 1697 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1697 Pro Ser Arg Ser Ser Lys Ile Thr His Arg 1 5 10 <210> 1698 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1698 Ser Thr Gly Arg Asn Gly Phe Lys Ser His 1 5 10 <210> 1699 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1699 Ser Leu Gln Leu Pro Ser Arg Ser Ser Lys 1 5 10 <210> 1700 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1700 Pro Cys Ser Val Phe Ser Pro Val Ser Ala 1 5 10 <210> 1701 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1701 Asp Ser Gly Lys Glu Gln Gly His Thr Arg 1 5 10 <210> 1702 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1702 Leu Pro Ser Arg Ser Ser Lys Ile Thr His 1 5 10 <210> 1703 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1703 Val Ser Leu Gln Leu Pro Ser Arg Ser Ser 1 5 10 <210> 1704 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1704 Ala Leu Gln Leu Asn Asn Arg Gln Ile Arg 1 5 10 <210> 1705 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1705 Leu Ser Ser Thr Gly Arg Asn Gly Phe Lys 1 5 10 <210> 1706 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1706 Asp Val Ser Leu Gln Leu Pro Ser Arg Ser 1 5 10 <210> 1707 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1707 Leu Asn Val Thr Leu Ser Ser Thr Gly Arg 1 5 10 <210> 1708 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1708 His Tyr Leu Pro Phe Ser Leu Pro His Arg 1 5 10 <210> 1709 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1709 Gly Ile Ser Leu Phe Asn Asn Pro Val Pro 1 5 10 <210> 1710 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1710 Leu Pro Gly Gly Tyr Gly Leu Pro Tyr Thr 1 5 10 <210> 1711 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1711 Leu Gly Gly Val Ala Ala Arg Pro Gly Phe 1 5 10 <210> 1712 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1712 Gly Ile Ala Glu Phe Pro Ser Arg Gly Lys 1 5 10 <210> 1713 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1713 Gly Ile Ala Glu Phe Pro Ser Arg Gly Lys 1 5 10 <210> 1714 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1714 Ser Gly Ile Gly Thr Leu Asp Gly Phe Arg 1 5 10 <210> 1715 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1715 Gly Ile Ala Glu Phe Pro Ser Arg Gly Lys 1 5 10 <210> 1716 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1716 Val Leu Ser Val Val Gly Thr Ala Trp Thr 1 5 10 <210> 1717 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1717 Leu Ser Val Val Gly Thr Ala Trp Thr Ala 1 5 10 <210> 1718 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1718 Leu Ser Val Val Gly Thr Ala Trp Thr Ala 1 5 10 <210> 1719 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1719 Ser Leu Phe Glu Tyr Gln Lys Asn Asn Lys 1 5 10 <210> 1720 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1720 Ser Val Val Gly Thr Ala Trp Thr Ala Asp 1 5 10 <210> 1721 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1721 Gly Ile Ala Glu Phe Pro Ser Arg Gly Lys 1 5 10 <210> 1722 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1722 Val Leu Ser Val Val Gly Thr Ala Trp Thr 1 5 10 <210> 1723 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1723 Val Pro Asp Leu Val Pro Gly Asn Phe Lys 1 5 10 <210> 1724 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1724 Val Val Gly Thr Ala Trp Thr Ala Asp Ser 1 5 10 <210> 1725 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1725 Gly Ser Trp Asn Ser Gly Ser Ser Gly Pro 1 5 10 <210> 1726 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1726 Val Gly Thr Ala Trp Thr Ala Asp Ser Gly 1 5 10 <210> 1727 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1727 Gly Ile Ala Glu Phe Pro Ser Arg Gly Lys 1 5 10 <210> 1728 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1728 Gly Ile Ala Glu Phe Pro Ser Arg Gly Lys 1 5 10 <210> 1729 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1729 Val Leu Ser Val Val Gly Thr Ala Trp Thr 1 5 10 <210> 1730 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1730 Pro Asp Leu Val Pro Gly Asn Phe Lys Ser 1 5 10 <210> 1731 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1731 Gln His Leu Pro Leu Ile Lys Met Lys Pro 1 5 10 <210> 1732 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1732 Thr Ala Trp Thr Ala Asp Ser Gly Glu Gly 1 5 10 <210> 1733 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1733 Val Leu Ser Val Val Gly Thr Ala Trp Thr 1 5 10 <210> 1734 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1734 Ala Phe Phe Asp Thr Ala Ser Thr Gly Lys 1 5 10 <210> 1735 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1735 Arg Asp Arg Gln His Leu Pro Leu Ile Lys 1 5 10 <210> 1736 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1736 Arg Asp Arg Gln His Leu Pro Leu Ile Lys 1 5 10 <210> 1737 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1737 Arg Asn Pro Ser Ser Ala Gly Ser Trp Asn 1 5 10 <210> 1738 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1738 Arg Asp Arg Gln His Leu Pro Leu Ile Lys 1 5 10 <210> 1739 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1739 Phe Phe Ser Pro Met Leu Gly Glu Phe Val 1 5 10 <210> 1740 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1740 Leu Ser Val Val Gly Thr Ala Trp Thr Ala 1 5 10 <210> 1741 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1741 Ser Leu Phe Glu Tyr Gln Lys Asn Asn Lys 1 5 10 <210> 1742 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1742 Val Leu Ser Val Val Gly Thr Ala Trp Thr 1 5 10 <210> 1743 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1743 Arg Asp Arg Gln His Leu Pro Leu Ile Lys 1 5 10 <210> 1744 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1744 Ser Val Ser Gly Ser Thr Gly Gln Trp His 1 5 10 <210> 1745 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1745 Gln His Leu Pro Leu Ile Lys Met Lys Pro 1 5 10 <210> 1746 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1746 Leu Thr Asp Met Pro Gln Met Arg Met Glu 1 5 10 <210> 1747 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1747 Leu Pro Leu Ile Lys Met Lys Pro Val Pro 1 5 10 <210> 1748 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1748 Arg Asp Arg Gln His Leu Pro Leu Ile Lys 1 5 10 <210> 1749 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1749 Val Leu Ser Val Val Gly Thr Ala Trp Thr 1 5 10 <210> 1750 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1750 Val Pro Asp Leu Val Pro Gly Asn Phe Lys 1 5 10 <210> 1751 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1751 Ile Ala Glu Phe Pro Ser Arg Gly Lys Ser 1 5 10 <210> 1752 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1752 Pro Gly Phe Phe Ser Pro Met Leu Gly Glu 1 5 10 <210> 1753 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1753 Leu Thr Asp Met Pro Gln Met Arg Met Glu 1 5 10 <210> 1754 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1754 Ser Arg Gly Lys Ser Ser Ser Tyr Ser Lys 1 5 10 <210> 1755 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1755 Ala Gly His Trp Thr Ser Glu Ser Ser Val 1 5 10 <210> 1756 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1756 Ser Gly Ile Gly Thr Leu Asp Gly Phe Arg 1 5 10 <210> 1757 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1757 Arg Asp Arg Gln His Leu Pro Leu Ile Lys 1 5 10 <210> 1758 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1758 Arg Pro Asn Asn Pro Asp Trp Gly Thr Phe 1 5 10 <210> 1759 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1759 Leu Thr Asp Met Pro Gln Met Arg Met Glu 1 5 10 <210> 1760 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1760 Arg His Arg His Pro Asp Glu Ala Ala Phe 1 5 10 <210> 1761 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1761 Gly Ile Ala Glu Phe Pro Ser Arg Gly Lys 1 5 10 <210> 1762 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1762 Arg Asp Arg Gln His Leu Pro Leu Ile Lys 1 5 10 <210> 1763 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1763 Pro Val Ser Leu Ala Glu Asp Pro Gln Gly 1 5 10 <210> 1764 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1764 Val Lys Phe Asn Lys Pro Phe Val Phe Leu 1 5 10 <210> 1765 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1765 Thr Glu Ala Ala Gly Ala Met Phe Leu Glu 1 5 10 <210> 1766 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1766 Ala Met Phe Leu Glu Ala Ile Pro Met Ser 1 5 10 <210> 1767 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1767 Leu Thr Ile Asp Glu Lys Gly Thr Glu Ala 1 5 10 <210> 1768 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1768 Gly Ala Met Phe Leu Glu Ala Ile Pro Met 1 5 10 <210> 1769 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1769 Glu Val Lys Phe Asn Lys Pro Phe Val Phe 1 5 10 <210> 1770 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1770 Ile Pro Met Ser Ile Pro Pro Glu Val Lys 1 5 10 <210> 1771 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1771 Gly Thr Glu Ala Ala Gly Ala Met Phe Leu 1 5 10 <210> 1772 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1772 Leu Cys Cys Leu Val Pro Val Ser Leu Ala 1 5 10 <210> 1773 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1773 Lys Phe Asn Lys Pro Phe Val Phe Leu Met 1 5 10 <210> 1774 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1774 Asp Glu Lys Gly Thr Glu Ala Ala Gly Ala 1 5 10 <210> 1775 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1775 Ala Gly Ala Met Phe Leu Glu Ala Ile Pro 1 5 10 <210> 1776 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1776 Glu Lys Gly Thr Glu Ala Ala Gly Ala Met 1 5 10 <210> 1777 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1777 Pro Val Ser Leu Ala Glu Asp Pro Gln Gly 1 5 10 <210> 1778 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1778 Lys Ala Val Leu Thr Ile Asp Glu Lys Gly 1 5 10 <210> 1779 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1779 Ala Val Leu Thr Ile Asp Glu Lys Gly Thr 1 5 10 <210> 1780 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1780 Gly Thr Glu Ala Ala Gly Ala Met Phe Leu 1 5 10 <210> 1781 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1781 Leu Cys Cys Leu Val Pro Val Ser Leu Ala 1 5 10 <210> 1782 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1782 Leu Cys Cys Leu Val Pro Val Ser Leu Ala 1 5 10 <210> 1783 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1783 Val Leu Thr Ile Asp Glu Lys Gly Thr Glu 1 5 10 <210> 1784 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1784 Pro Val Ser Leu Ala Glu Asp Pro Gln Gly 1 5 10 <210> 1785 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1785 Thr Ile Asp Glu Lys Gly Thr Glu Ala Ala 1 5 10 <210> 1786 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1786 His Lys Ala Val Leu Thr Ile Asp Glu Lys 1 5 10 <210> 1787 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1787 Ile Asp Glu Lys Gly Thr Glu Ala Ala Gly 1 5 10 <210> 1788 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1788 Leu Cys Cys Leu Val Pro Val Ser Leu Ala 1 5 10 <210> 1789 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1789 Cys Leu Val Pro Val Ser Leu Ala Glu Asp 1 5 10 <210> 1790 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1790 Ala Ser Ser Phe Phe Thr Leu Ser Leu Gln 1 5 10 <210> 1791 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1791 Ala Ser Ser Phe Phe Thr Leu Ser Leu Gln 1 5 10 <210> 1792 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1792 Ala Ser Ser Phe Phe Thr Leu Ser Leu Gln 1 5 10 <210> 1793 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1793 Ala Ser Ser Phe Phe Thr Leu Ser Leu Gln 1 5 10 <210> 1794 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1794 Ala Ser Ser Phe Phe Thr Leu Ser Leu Gln 1 5 10 <210> 1795 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1795 Ala Ser Ser Phe Phe Thr Leu Ser Leu Gln 1 5 10 <210> 1796 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1796 Ala Ser Ser Phe Phe Thr Leu Ser Leu Gln 1 5 10 <210> 1797 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1797 Ala Ser Ser Phe Phe Thr Leu Ser Leu Gln 1 5 10 <210> 1798 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1798 Leu Asn Val Thr Leu Ser Ser Thr Gly Arg 1 5 10 <210> 1799 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1799 Ala Ser Ser Phe Phe Thr Leu Ser Leu Gln 1 5 10 <210> 1800 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1800 Leu Asn Val Thr Leu Ser Ser Thr Gly Arg 1 5 10 <210> 1801 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1801 Asp Tyr Glu Tyr Asp Glu Leu Pro Ala Lys 1 5 10 <210> 1802 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1802 Ala Ser Ser Phe Phe Thr Leu Ser Leu Gln 1 5 10 <210> 1803 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1803 Ala Leu Gln Leu Asn Asn Arg Gln Ile Arg 1 5 10 <210> 1804 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1804 Tyr Glu Tyr Asp Glu Leu Pro Ala Lys Asp 1 5 10 <210> 1805 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1805 Asp Tyr Glu Tyr Asp Glu Leu Pro Ala Lys 1 5 10 <210> 1806 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1806 Asn Val Thr Leu Ser Ser Thr Gly Arg Asn 1 5 10 <210> 1807 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1807 Asp Tyr Glu Tyr Asp Glu Leu Pro Ala Lys 1 5 10 <210> 1808 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1808 Ala Ser Ser Phe Phe Thr Leu Ser Leu Gln 1 5 10 <210> 1809 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1809 Asp Tyr Glu Tyr Asp Glu Leu Pro Ala Lys 1 5 10 <210> 1810 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1810 Ala Leu Gln Leu Asn Asn Arg Gln Ile Arg 1 5 10 <210> 1811 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1811 Glu Leu Asn Pro Leu Asp His Arg Gly Arg 1 5 10 <210> 1812 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1812 Thr Leu Ser Leu Gln Lys Pro Arg Leu Leu 1 5 10 <210> 1813 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1813 Ile Ile Pro Gln Thr Ile Ser Glu Leu Gln 1 5 10 <210> 1814 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1814 Ser Pro His Pro Ala Ile Ala Arg Leu Thr 1 5 10 <210> 1815 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1815 Thr Leu Ser Leu Gln Lys Pro Arg Leu Leu 1 5 10 <210> 1816 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1816 Glu Tyr Asp Glu Leu Pro Ala Lys Asp Asp 1 5 10 <210> 1817 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1817 Tyr Glu Tyr Asp Glu Leu Pro Ala Lys Asp 1 5 10 <210> 1818 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1818 Leu Ser Leu Gln Lys Pro Arg Leu Leu Leu 1 5 10 <210> 1819 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1819 Ala Asn Glu Asp Tyr Glu Asp Tyr Glu Tyr 1 5 10 <210> 1820 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1820 Thr Leu Ser Leu Gln Lys Pro Arg Leu Leu 1 5 10 <210> 1821 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1821 Thr Leu Ser Leu Gln Lys Pro Arg Leu Leu 1 5 10 <210> 1822 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1822 His Pro Ala Ile Ala Arg Leu Thr Val Ala 1 5 10 <210> 1823 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1823 Arg Gly His Arg Pro Leu Asp Lys Lys Arg 1 5 10 <210> 1824 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1824 Gly His Arg Pro Leu Asp Lys Lys Arg Glu 1 5 10 <210> 1825 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1825 Ala Arg Gly His Arg Pro Leu Asp Lys Lys 1 5 10 <210> 1826 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1826 Leu Leu Leu Cys Val Phe Leu Val Lys Ser 1 5 10 <210> 1827 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1827 Leu Leu Leu Cys Val Phe Leu Val Lys Ser 1 5 10 <210> 1828 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1828 Leu Leu Leu Cys Val Phe Leu Val Lys Ser 1 5 10 <210> 1829 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1829 Leu Leu Leu Cys Val Phe Leu Val Lys Ser 1 5 10 <210> 1830 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1830 Leu Leu Leu Cys Val Phe Leu Val Lys Ser 1 5 10 <210> 1831 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1831 Ser Ala Arg Gly His Arg Pro Leu Asp Lys 1 5 10 <210> 1832 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1832 Leu Leu Leu Cys Val Phe Leu Val Lys Ser 1 5 10 <210> 1833 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1833 Leu Leu Leu Cys Val Phe Leu Val Lys Ser 1 5 10 <210> 1834 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1834 Phe Phe Ser Ala Arg Gly His Arg Pro Leu 1 5 10 <210> 1835 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1835 Leu Leu Leu Cys Val Phe Leu Val Lys Ser 1 5 10 <210> 1836 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1836 Cys Val Phe Leu Val Lys Ser Gln Gly Val 1 5 10 <210> 1837 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1837 Leu Leu Leu Cys Val Phe Leu Val Lys Ser 1 5 10 <210> 1838 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1838 Leu Leu Leu Cys Val Phe Leu Val Lys Ser 1 5 10 <210> 1839 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1839 Leu Cys Val Phe Leu Val Lys Ser Gln Gly 1 5 10 <210> 1840 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1840 Leu Cys Val Phe Leu Val Lys Ser Gln Gly 1 5 10 <210> 1841 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1841 Leu Cys Val Phe Leu Val Lys Ser Gln Gly 1 5 10 <210> 1842 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1842 Leu Leu Leu Cys Val Phe Leu Val Lys Ser 1 5 10 <210> 1843 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1843 Leu Leu Leu Cys Val Phe Leu Val Lys Ser 1 5 10 <210> 1844 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1844 Leu Leu Leu Cys Val Phe Leu Val Lys Ser 1 5 10 <210> 1845 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1845 Leu Cys Val Phe Leu Val Lys Ser Gln Gly 1 5 10 <210> 1846 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1846 Ser Ala Arg Gly His Arg Pro Leu Asp Lys 1 5 10 <210> 1847 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1847 Asp Asn Glu Glu Gly Phe Phe Ser Ala Arg 1 5 10 <210> 1848 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1848 Cys Val Phe Leu Val Lys Ser Gln Gly Val 1 5 10 <210> 1849 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1849 Leu Leu Leu Cys Val Phe Leu Val Lys Ser 1 5 10 <210> 1850 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1850 Leu Leu Leu Cys Val Phe Leu Val Lys Ser 1 5 10 <210> 1851 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1851 Trp Tyr Ser Met Arg Lys Met Ser Met Lys 1 5 10 <210> 1852 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1852 Val Phe Leu Val Lys Ser Gln Gly Val Asn 1 5 10 <210> 1853 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1853 Leu Leu Leu Cys Val Phe Leu Val Lys Ser 1 5 10 <210> 1854 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1854 Leu Leu Leu Cys Val Phe Leu Val Lys Ser 1 5 10 <210> 1855 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1855 Leu Leu Leu Cys Val Phe Leu Val Lys Ser 1 5 10 <210> 1856 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1856 Ile Ser Asp Ala Arg Glu Asn Ile Gln Arg 1 5 10 <210> 1857 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1857 Gly Pro Gly Gly Val Trp Ala Ala Glu Ala 1 5 10 <210> 1858 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1858 Gln Arg Phe Phe Gly His Gly Ala Glu Asp 1 5 10 <210> 1859 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1859 Ser Asp Ala Arg Glu Asn Ile Gln Arg Phe 1 5 10 <210> 1860 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1860 Phe Cys Ser Leu Val Leu Gly Val Ser Ser 1 5 10 <210> 1861 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1861 Ala Asn Glu Trp Gly Arg Ser Gly Lys Asp 1 5 10 <210> 1862 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1862 Ala Lys Arg Gly Pro Gly Gly Val Trp Ala 1 5 10 <210> 1863 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1863 Gly Ala Glu Asp Ser Leu Ala Asp Gln Ala 1 5 10 <210> 1864 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1864 Ser Phe Phe Ser Phe Leu Gly Glu Ala Phe 1 5 10 <210> 1865 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1865 Gly Val Trp Ala Ala Glu Ala Ile Ser Asp 1 5 10 <210> 1866 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1866 Cys Ser Leu Val Leu Ser Val Ser Ser Arg 1 5 10 <210> 1867 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1867 Phe Gly His Gly Ala Glu Asp Ser Leu Ala 1 5 10 <210> 1868 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1868 Leu Ser Val Ser Ser Arg Ser Phe Phe Ser 1 5 10 <210> 1869 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1869 Gly His Gly Ala Glu Asp Ser Leu Ala Asp 1 5 10 <210> 1870 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1870 Ala Ile Ser Asp Ala Arg Glu Asn Ile Gln 1 5 10 <210> 1871 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1871 Ile Ser Asp Ala Arg Glu Asn Ile Gln Arg 1 5 10 <210> 1872 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1872 Arg Glu Asn Ile Gln Arg Phe Phe Gly His 1 5 10 <210> 1873 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1873 Ala Ala Asn Glu Trp Gly Arg Ser Gly Lys 1 5 10 <210> 1874 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1874 Ala Arg Glu Asn Ile Gln Arg Phe Phe Gly 1 5 10 <210> 1875 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1875 Ala Asp Gln Ala Ala Asn Glu Trp Gly Arg 1 5 10 <210> 1876 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1876 Ala Glu Asp Ser Leu Ala Asp Gln Ala Ala 1 5 10 <210> 1877 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1877 Gly Gly Val Trp Ala Ala Glu Ala Ile Ser 1 5 10 <210> 1878 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1878 Val Leu Ser Val Ser Ser Arg Ser Phe Phe 1 5 10 <210> 1879 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1879 Phe Gly His Gly Ala Glu Asp Ser Leu Ala 1 5 10 <210> 1880 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1880 Gly Val Trp Ala Ala Glu Ala Ile Ser Asp 1 5 10 <210> 1881 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1881 Phe Phe Gly His Gly Ala Glu Asp Ser Leu 1 5 10 <210> 1882 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1882 Pro Gly Gly Val Trp Ala Ala Glu Ala Ile 1 5 10 <210> 1883 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1883 Val Ser Ser Arg Ser Phe Phe Ser Phe Leu 1 5 10 <210> 1884 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1884 Ile Gly Ser Asp Lys Tyr Phe His Ala Arg 1 5 10 <210> 1885 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1885 Phe Cys Ser Leu Val Leu Gly Val Ser Ser 1 5 10 <210> 1886 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1886 Gly Asn Tyr Asp Ala Ala Lys Arg Gly Pro 1 5 10 <210> 1887 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1887 Glu His Ala Glu Val Val Val Phe Thr Ala Asn 1 5 10 <210> 1888 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1888 Ala Glu Val Val Phe Thr Ala Asn Asp Ser 1 5 10 <210> 1889 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1889 Ala Glu Val Val Phe Thr Ala Asn Asp Ser 1 5 10 <210> 1890 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1890 His Ala Glu Val Val Phe Thr Ala Asn Asp 1 5 10 <210> 1891 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1891 Glu Val Val Phe Thr Ala Asn Asp Ser Gly 1 5 10 <210> 1892 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1892 Pro Arg Arg Tyr Thr Ile Ala Ala Leu Leu 1 5 10 <210> 1893 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1893 Asp Ser Gly Pro Arg Arg Tyr Thr Ile Ala 1 5 10 <210> 1894 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1894 Ala Asn Asp Ser Gly Pro Arg Arg Tyr Thr 1 5 10 <210> 1895 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1895 Pro Phe His Glu His Ala Glu Val Val Phe 1 5 10 <210> 1896 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1896 Asp Thr Lys Ser Tyr Trp Lys Ala Leu Gly 1 5 10 <210> 1897 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1897 Pro Cys Ser Val Phe Ser Pro Val Ser Ala 1 5 10 <210> 1898 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1898 Pro Cys Ser Val Phe Ser Pro Val Ser Ala 1 5 10 <210> 1899 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1899 Pro Leu Gly Arg Gln Leu Thr Ser Gly Pro 1 5 10 <210> 1900 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1900 Gly Asp Lys Leu Phe Gly Pro Asp Leu Lys 1 5 10 <210> 1901 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1901 Ala Met Glu Pro Leu Gly Arg Gln Leu Thr 1 5 10 <210> 1902 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1902 Pro Cys Ser Val Phe Ser Pro Val Ser Ala 1 5 10 <210> 1903 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1903 Cys Ser Val Phe Ser Pro Val Ser Ala Met 1 5 10 <210> 1904 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1904 Pro Leu Gly Arg Gln Leu Thr Ser Gly Pro 1 5 10 <210> 1905 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1905 Pro Leu Gly Arg Gln Leu Thr Ser Gly Pro 1 5 10 <210> 1906 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1906 Ala Ala Ala Thr Ser Ile Ala Met Ser Arg 1 5 10 <210> 1907 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1907 Pro Cys Ser Val Phe Ser Pro Val Ser Ala 1 5 10 <210> 1908 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1908 Glu Asp Leu Arg Gln Gly Leu Leu Pro Val 1 5 10 <210> 1909 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1909 Asp Leu Arg Gln Gly Leu Leu Pro Val Leu 1 5 10 <210> 1910 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1910 Pro Gln Ser Pro Trp Asp Arg Val Lys Asp 1 5 10 <210> 1911 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1911 Gly Ser Gln Ala Arg His Phe Trp Gln Gln 1 5 10 <210> 1912 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1912 Leu Arg Gln Gly Leu Leu Pro Val Leu Glu 1 5 10 <210> 1913 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1913 Gly Leu Leu Pro Val Leu Glu Ser Phe Lys 1 5 10 <210> 1914 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1914 Leu Gly Pro Val Thr Gln Glu Phe Trp Asp 1 5 10 <210> 1915 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1915 Val Leu Glu Ser Phe Lys Val Ser Phe Leu 1 5 10 <210> 1916 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1916 Leu Leu Pro Val Leu Glu Ser Phe Lys Val 1 5 10 <210> 1917 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1917 Gly Ser Gln Ala Arg His Phe Trp Gln Gln 1 5 10 <210> 1918 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1918 Leu Tyr Arg Gln Lys Val Glu Pro Leu Arg 1 5 10 <210> 1919 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1919 Leu Tyr Arg Gln Lys Val Glu Pro Leu Arg 1 5 10 <210> 1920 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1920 Gly Ser Gln Ala Arg His Phe Trp Gln Gln 1 5 10 <210> 1921 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1921 Thr Ala Val Lys Ile Thr Leu Leu Ser Ala 1 5 10 <210> 1922 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1922 Ala Ala Thr Ala Val Lys Ile Thr Leu Leu 1 5 10 <210> 1923 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1923 Ala Val Lys Ile Thr Leu Leu Ser Ala Leu 1 5 10 <210> 1924 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1924 Lys Ile Thr Leu Leu Ser Ala Leu Val Glu 1 5 10 <210> 1925 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1925 Pro Phe Leu Met Ile Ile Val Pro Thr Asp 1 5 10 <210> 1926 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1926 Ala Thr Ala Val Lys Ile Thr Leu Leu Ser 1 5 10 <210> 1927 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1927 Gly Phe Cys Pro Ala Val Leu Cys His Pro 1 5 10 <210> 1928 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1928 Ile Val Arg Phe Asn Arg Pro Phe Leu Met 1 5 10 <210> 1929 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1929 Ala Ala Gly Phe Cys Pro Ala Val Leu Cys 1 5 10 <210> 1930 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1930 Phe Val Met Leu Val Gln Gly Ser Trp Gln 1 5 10 <210> 1931 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1931 Phe Val Met Leu Val Gln Gly Ser Trp Gln 1 5 10 <210> 1932 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1932 Met Leu Val Gln Gly Ser Trp Gln Arg Ser 1 5 10 <210> 1933 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1933 Val Met Leu Val Gln Gly Ser Trp Gln Arg 1 5 10 <210> 1934 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1934 Asp Pro Asp Gln Met Asn Glu Asp Lys Arg 1 5 10 <210> 1935 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1935 Met Leu Val Gln Gly Ser Trp Gln Arg Ser 1 5 10 <210> 1936 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1936 Asp Pro Asp Gln Met Asn Glu Asp Lys Arg 1 5 10 <210> 1937 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1937 Leu Val Gln Gly Ser Trp Gln Arg Ser Leu 1 5 10 <210> 1938 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1938 Val Met Leu Val Gln Gly Ser Trp Gln Arg 1 5 10 <210> 1939 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1939 Ala Trp Leu Val Lys Gly Arg Gly Arg Arg 1 5 10 <210> 1940 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1940 Lys Arg Asn Arg Asn Asn Ile Ala Lys Arg 1 5 10 <210> 1941 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1941 Leu Leu Leu Leu Ala Ser Leu Thr Ser Gly 1 5 10 <210> 1942 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1942 Leu Leu Leu Leu Ala Ser Leu Thr Ser Gly 1 5 10 <210> 1943 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1943 Leu Leu Leu Leu Ala Ser Leu Thr Ser Gly 1 5 10 <210> 1944 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1944 Leu Leu Leu Leu Ala Ser Leu Thr Ser Gly 1 5 10 <210> 1945 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1945 Leu Leu Leu Leu Ala Ser Leu Thr Ser Gly 1 5 10 <210> 1946 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1946 Leu Leu Leu Leu Ala Ser Leu Thr Ser Gly 1 5 10 <210> 1947 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1947 Ala Ser Leu Thr Ser Gly Ser Val Phe Pro 1 5 10 <210> 1948 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1948 Leu Leu Leu Ala Ser Leu Thr Ser Gly Ser 1 5 10 <210> 1949 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1949 Ala Ser Leu Thr Ser Gly Ser Val Phe Pro 1 5 10 <210> 1950 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1950 Leu Leu Leu Leu Ala Ser Leu Thr Ser Gly 1 5 10 <210> 1951 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1951 Leu Leu Leu Leu Ala Ser Leu Thr Ser Gly 1 5 10 <210> 1952 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1952 Leu Leu Leu Leu Ala Ser Leu Thr Ser Gly 1 5 10 <210> 1953 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1953 Gly Pro Asn Ala Arg Glu Asn Ile Gln Arg 1 5 10 <210> 1954 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1954 Pro Asn Ala Arg Glu Asn Ile Gln Arg Leu 1 5 10 <210> 1955 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1955 Ala Ala Asn Lys Trp Gly Arg Ser Gly Arg 1 5 10 <210> 1956 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1956 Asn Ala Arg Glu Asn Ile Gln Arg Leu Thr 1 5 10 <210> 1957 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1957 Pro Asn Ala Arg Glu Asn Ile Gln Arg Leu 1 5 10 <210> 1958 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1958 Gly Pro Asn Ala Arg Glu Asn Ile Gln Arg 1 5 10 <210> 1959 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1959 Gln Arg Leu Thr Gly Arg Gly Ala Glu Asp 1 5 10 <210> 1960 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1960 Ala Arg Glu Asn Ile Gln Arg Leu Thr Gly 1 5 10 <210> 1961 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1961 Glu Asn Ile Gln Arg Leu Thr Gly Arg Gly 1 5 10 <210> 1962 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1962 Ala Arg Gly Asn Tyr Asp Ala Ala Lys Arg 1 5 10 <210> 1963 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1963 Ala Lys Arg Gly Pro Gly Gly Ala Trp Ala 1 5 10 <210> 1964 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1964 Thr Gly Arg Gly Ala Glu Asp Ser Leu Ala 1 5 10 <210> 1965 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1965 Lys Arg Gly Pro Gly Gly Ala Trp Ala Ala 1 5 10 <210> 1966 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1966 Asp Lys Ser Lys Leu Lys Lys Thr Glu Thr 1 5 10 <210> 1967 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1967 Phe Asp Lys Ser Lys Leu Lys Lys Thr Glu 1 5 10 <210> 1968 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1968 Ser Lys Leu Lys Lys Thr Glu Thr Gln Glu 1 5 10 <210> 1969 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1969 Glu Lys Phe Asp Lys Ser Lys Leu Lys Lys 1 5 10 <210> 1970 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1970 Lys Ser Lys Leu Lys Lys Thr Glu Thr Gln 1 5 10 <210> 1971 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1971 Lys Leu Lys Lys Thr Glu Thr Gln Glu Lys 1 5 10 <210> 1972 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1972 Pro Lys Asn Pro Ala Asn Pro Val Gln Arg 1 5 10 <210> 1973 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1973 Pro Lys Asn Pro Ala Asn Pro Val Gln Arg 1 5 10 <210> 1974 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1974 Cys Ala Val Ala Glu Tyr Gly Val Tyr Val 1 5 10 <210> 1975 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1975 Pro Lys Asn Pro Ala Asn Pro Val Gln Arg 1 5 10 <210> 1976 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1976 Pro Lys Asn Pro Ala Asn Pro Val Gln Arg 1 5 10 <210> 1977 <211> 5 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1977 Met Ser Ala Leu Gly 1 5 <210> 1978 <211> 4 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1978 Met Ser Ala Leu One <210> 1979 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1979 Asn Phe Lys Leu Leu Ser His Cys Leu Leu 1 5 10 <210> 1980 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1980 Lys Leu Leu Ser His Cys Leu Leu Val Thr 1 5 10 <210> 1981 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1981 Phe Thr Pro Ala Val His Ala Ser Leu Asp 1 5 10 <210> 1982 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1982 Leu Leu Ser His Cys Leu Leu Val Thr Leu 1 5 10 <210> 1983 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1983 Val Ala Leu Glu Gln Ala Gln Lys Val Arg 1 5 10 <210> 1984 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1984 Ala Gln Lys Val Arg Tyr Glu Gly Ser Tyr 1 5 10 <210> 1985 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1985 Glu Gln Ala Gln Lys Val Arg Tyr Glu Gly 1 5 10 <210> 1986 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1986 Pro Asp Ala Pro Pro Ser Pro Pro Leu Gly 1 5 10 <210> 1987 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1987 Gly Glu Val Ser His Pro Arg Lys Thr Arg 1 5 10 <210> 1988 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1988 Pro Asp Ala Pro Pro Ser Pro Pro Leu Gly 1 5 10 <210> 1989 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1989 Gly Ser Pro Pro Asp Ser His Val Leu Leu 1 5 10 <210> 1990 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1990 Pro Asp Ala Pro Pro Ser Pro Pro Leu Gly 1 5 10 <210> 1991 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1991 Ser Pro Pro Asp Ser His Val Leu Leu Ala 1 5 10 <210> 1992 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1992 Pro Asp Ala Pro Pro Ser Pro Pro Leu Gly 1 5 10 <210> 1993 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1993 Gly Ser Pro Pro Asp Ser His Val Leu Leu 1 5 10 <210> 1994 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1994 Ala Lys Glu Arg Ala His Gln Gln Lys Lys 1 5 10 <210> 1995 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1995 Ala Lys Glu Arg Ala His Gln Gln Lys Lys 1 5 10 <210> 1996 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1996 Leu Glu Ala Gly Leu Pro Leu Gln Val Arg 1 5 10 <210> 1997 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1997 Ala Lys Glu Arg Ala His Gln Gln Lys Lys 1 5 10 <210> 1998 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1998 Leu Ala Lys Glu Leu Thr Ala Glu Lys Arg 1 5 10 <210> 1999 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 1999 Leu Ala Lys Glu Leu Thr Ala Glu Lys Arg 1 5 10 <210> 2000 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2000 Leu Asp Val Ser Leu Gln Leu Pro Ser Arg 1 5 10 <210> 2001 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2001 Leu Asp Val Ser Leu Gln Leu Pro Ser Arg 1 5 10 <210> 2002 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2002 Leu Gln Leu Pro Ser Arg Ser Ser Lys Ile 1 5 10 <210> 2003 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2003 Val Ser Leu Gln Leu Pro Ser Arg Ser Ser 1 5 10 <210> 2004 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2004 Leu Leu Thr His Leu Pro Leu Ala Leu Gly 1 5 10 <210> 2005 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2005 Leu Pro Ser Arg Ser Ser Lys Ile Thr His 1 5 10 <210> 2006 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2006 Gln Leu Pro Ser Arg Ser Ser Lys Ile Thr 1 5 10 <210> 2007 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2007 Ser Arg Ser Ser Lys Ile Thr His Arg Ile 1 5 10 <210> 2008 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2008 Pro Ser Arg Ser Ser Lys Ile Thr His Arg 1 5 10 <210> 2009 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2009 Asp Ile Phe Glu Leu Leu Phe Trp Gly Arg 1 5 10 <210> 2010 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2010 Leu Leu Phe Trp Gly Arg Thr Ser Ala Gly 1 5 10 <210> 2011 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2011 Gln Val Gly Gly Pro Ser Leu Thr Ser Asp 1 5 10 <210> 2012 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2012 Asp Ser Trp Glu Asp Ile Phe Glu Leu Leu 1 5 10 <210> 2013 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2013 Leu Leu Phe Trp Gly Arg Thr Ser Ala Gly 1 5 10 <210> 2014 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2014 Asp Ile Phe Glu Leu Leu Phe Trp Gly Arg 1 5 10 <210> 2015 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2015 Asp Ser Trp Glu Asp Ile Phe Glu Leu Leu 1 5 10 <210> 2016 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2016 Val Asp Ala Ala Phe Arg Gln Gly His Asn 1 5 10 <210> 2017 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2017 Val Asp Ala Ala Phe Arg Gln Gly His Asn 1 5 10 <210> 2018 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2018 Val Asp Ala Ala Phe Arg Gln Gly His Asn 1 5 10 <210> 2019 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2019 Arg Glu Leu Ile Ser Glu Arg Trp Lys Asn 1 5 10 <210> 2020 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2020 Val Asp Ala Ala Phe Arg Gln Gly His Asn 1 5 10 <210> 2021 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2021 Val Phe Leu Ile Lys Gly Asp Lys Val Trp 1 5 10 <210> 2022 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2022 Pro Ala Pro Ala Gln Ser Gln Thr Gln Phe 1 5 10 <210> 2023 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2023 His Val Gln Ser Gln Thr Gln Pro Val Ser 1 5 10 <210> 2024 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2024 Pro Ala Pro Ala Gln Ser Gln Thr Gln Phe 1 5 10 <210> 2025 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2025 Pro Ala Pro Ala Gln Ser Gln Thr Gln Phe 1 5 10 <210> 2026 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2026 Phe Gly Pro Val Val Ala Pro Lys Pro Lys 1 5 10 <210> 2027 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2027 Leu Leu Ala Leu Leu Ala Ser Ala Arg Ala 1 5 10 <210> 2028 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2028 Leu Leu Ala Leu Leu Ala Ser Ala Arg Ala 1 5 10 <210> 2029 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2029 Ser Thr Val Lys Asp Lys Phe Ser Glu Phe 1 5 10 <210> 2030 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2030 Leu Leu Ala Leu Leu Ala Ser Ala Arg Ala 1 5 10 <210> 2031 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2031 Asp Lys Phe Ser Glu Phe Trp Asp Leu Asp 1 5 10 <210> 2032 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2032 Lys Leu Ala Pro Val Ser Lys Arg Phe Pro 1 5 10 <210> 2033 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2033 Thr Asp Lys Leu Ala Pro Val Ser Lys Arg 1 5 10 <210> 2034 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2034 Lys Leu Ala Pro Val Ser Lys Arg Phe Pro 1 5 10 <210> 2035 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2035 Ile Asn Ser Asn Gln Val Lys Arg Val Pro 1 5 10 <210> 2036 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2036 Glu Ile Ile Asn Ser Asn Gln Val Lys Arg 1 5 10 <210> 2037 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2037 Leu Ser Lys Ser Gly Tyr Pro Lys Thr Pro 1 5 10 <210> 2038 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2038 Glu Thr Gln Gln Trp Pro Glu Arg Lys Leu 1 5 10 <210> 2039 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2039 Glu Pro Thr Glu Ser Thr Gln Gln Leu Asn 1 5 10 <210> 2040 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2040 Leu Glu Ala Asp Glu Arg Glu Pro Thr Glu 1 5 10 <210> 2041 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2041 Ala Asp Glu Arg Glu Pro Thr Glu Ser Thr 1 5 10 <210> 2042 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2042 Val Leu Thr Ser Leu Ser His Ala Phe Gly 1 5 10 <210> 2043 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2043 Val Leu Thr Ser Leu Ser His Ala Phe Gly 1 5 10 <210> 2044 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2044 Val Leu Thr Ser Leu Ser His Ala Phe Gly 1 5 10 <210> 2045 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2045 Ser Ala Tyr Ser Arg Gly Val Phe Arg Arg 1 5 10 <210> 2046 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2046 Ser Ala Tyr Ser Arg Gly Val Phe Arg Arg 1 5 10 <210> 2047 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2047 Ser Ala Tyr Ser Arg Gly Val Phe Arg Arg 1 5 10 <210> 2048 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2048 Glu Gly Lys Asn Val Ile Gly Leu Gln Met 1 5 10 <210> 2049 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2049 Gln Glu Gly Lys Asn Val Ile Gly Leu Gln 1 5 10 <210> 2050 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2050 Thr Asn Arg Gly Ala Ser Gln Ala Gly Met 1 5 10 <210> 2051 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2051 Met Leu Thr Arg Pro Arg Tyr Gly Lys Arg 1 5 10 <210> 2052 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2052 Gln Pro Leu Leu Gly Ala Gln Gly Ala Pro 1 5 10 <210> 2053 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2053 Val Ala Leu Leu Leu Gln Pro Leu Leu Gly 1 5 10 <210> 2054 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2054 Gln Pro Leu Leu Gly Ala Gln Gly Ala Pro 1 5 10 <210> 2055 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2055 Leu Ile Asn Gly Leu Gly Ala Ala Pro Pro 1 5 10 <210> 2056 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2056 Leu Ile Asn Gly Leu Gly Ala Ala Pro Pro 1 5 10 <210> 2057 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2057 Cys Leu Leu Leu Ile Asn Gly Leu Gly Ala 1 5 10 <210> 2058 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2058 Val Glu Glu Lys Arg Lys Arg Lys Lys Asn 1 5 10 <210> 2059 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2059 Glu Val Glu Glu Lys Arg Lys Arg Lys Lys 1 5 10 <210> 2060 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2060 Cys Leu Leu Leu Ile Asn Gly Leu Gly Ala 1 5 10 <210> 2061 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2061 Gly Ser Gln Gln Gly Pro Glu Glu Glu Ala 1 5 10 <210> 2062 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2062 Glu Val Glu Glu Lys Arg Lys Arg Lys Lys 1 5 10 <210> 2063 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2063 Arg Thr Pro Gly Ile Trp Leu Leu His Cys 1 5 10 <210> 2064 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2064 Leu Phe Leu Cys Ser Thr Pro Ala Trp Ala 1 5 10 <210> 2065 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2065 His Asn Arg Ser Ala Met Pro Phe Thr Ala 1 5 10 <210> 2066 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2066 Lys Gln Ser Thr Ser Phe Leu Val Leu Gln 1 5 10 <210> 2067 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2067 Thr Thr Ala Arg Val Ile Thr Asn Gln Tyr 1 5 10 <210> 2068 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2068 Pro Tyr Pro Arg Ile His Phe Pro Leu Ala 1 5 10 <210> 2069 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2069 Pro Tyr Pro Arg Ile His Phe Pro Leu Ala 1 5 10 <210> 2070 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2070 Pro Leu Ala Thr Tyr Ala Pro Val Ile Ser 1 5 10 <210> 2071 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2071 Glu Val Gly Gly Glu Ala Leu Gly Arg Leu 1 5 10 <210> 2072 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2072 Ser Asn Glu Gln Ala Thr Ser Leu Asn Thr 1 5 10 <210> 2073 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2073 Asn Glu Gln Ala Thr Ser Leu Asn Thr Val 1 5 10 <210> 2074 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2074 Ser Asn Glu Gln Ala Thr Ser Leu Asn Thr 1 5 10 <210> 2075 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2075 Lys Ser Asn Glu Gln Ala Thr Ser Leu Asn 1 5 10 <210> 2076 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2076 Ile Cys Phe Phe Leu Ser Glu Val Ser Gly 1 5 10 <210> 2077 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2077 Thr Ala Ala Ala Lys Arg Arg Ile Thr Arg 1 5 10 <210> 2078 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2078 Asp Gln Tyr Tyr Leu Arg Val Thr Thr Val 1 5 10 <210> 2079 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2079 Pro Val Glu Val Ser Arg Lys Asn Pro Lys 1 5 10 <210> 2080 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2080 Val Leu Glu Gly Pro Ala Pro Ala Gln Gly 1 5 10 <210> 2081 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2081 Glu Gly Pro Ala Pro Ala Gln Gly Thr Pro 1 5 10 <210> 2082 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2082 Lys Thr Ser Glu Val Lys Gln Leu Ile Lys 1 5 10 <210> 2083 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2083 Asn Trp Ile Gln Tyr Lys Glu Gly Phe Gly 1 5 10 <210> 2084 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2084 Met Lys Ile Ile Pro Phe Asn Arg Leu Thr 1 5 10 <210> 2085 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2085 Ala Arg Ser Val Ser Lys Arg Ser Arg Arg 1 5 10 <210> 2086 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2086 Arg Ser Val Ser Lys Arg Ser Arg Arg Glu 1 5 10 <210> 2087 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2087 Leu Leu Ser His Cys Thr Gly Ser Val Thr 1 5 10 <210> 2088 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2088 Leu Ser His Cys Thr Gly Ser Val Thr Ser 1 5 10 <210> 2089 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2089 Ser Glu Thr Val Cys Leu Cys Asn His Phe 1 5 10 <210> 2090 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2090 Ser Glu Thr Val Cys Leu Cys Asn His Phe 1 5 10 <210> 2091 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2091 Leu Thr Leu Cys Thr Gly Ser Glu Ala Ser 1 5 10 <210> 2092 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2092 Val Leu Ala Tyr Cys Thr Gly Ser Val Ala 1 5 10 <210> 2093 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2093 Leu Ile His Cys Thr Gly Ser Trp Ala Gln 1 5 10 <210> 2094 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2094 Cys Thr Gly Ser Trp Ala Gln Ser Val Leu 1 5 10 <210> 2095 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2095 Leu Ile Thr His Cys Ala Gly Ser Trp Ala 1 5 10 <210> 2096 <211> 11 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2096 Leu Ile Thr His Cys Ala Gly Ser Trp Ala Gln 1 5 10 <210> 2097 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2097 Cys Thr Gly Ser Val Ala Ser Tyr Glu Leu 1 5 10 <210> 2098 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2098 Leu Leu Gly Leu Leu Cys Gly Ser Val Ala 1 5 10 <210> 2099 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2099 Leu Leu Leu Trp Leu Pro Asp Thr Thr Gly 1 5 10 <210> 2100 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2100 Leu Leu Trp Leu Pro Asp Thr Thr Gly Glu 1 5 10 <210> 2101 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2101 Leu Met Leu Trp Val Pro Gly Ser Ser Gly 1 5 10 <210> 2102 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2102 Leu Met Leu Trp Val Pro Gly Ser Ser Gly 1 5 10 <210> 2103 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2103 Asp Asn Phe Pro Arg Tyr Pro Val Gly Lys 1 5 10 <210> 2104 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2104 Asp Asn Phe Pro Arg Tyr Pro Val Gly Lys 1 5 10 <210> 2105 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2105 Lys Ala Gly Thr Glu Leu Val Asn Phe Leu 1 5 10 <210> 2106 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2106 Glu Gln Leu Thr Pro Leu Ile Lys Lys Ala 1 5 10 <210> 2107 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2107 Ser Leu Val Ser Gln Tyr Phe Gln Thr Val 1 5 10 <210> 2108 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2108 Leu Met Leu Trp Val Pro Gly Ser Ser Gly 1 5 10 <210> 2109 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2109 Leu Met Leu Trp Val Pro Gly Ser Ser Gly 1 5 10 <210> 2110 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2110 Asp Arg Ala Ile Glu Gly Arg Thr Ala Thr 1 5 10 <210> 2111 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2111 Arg Ala Ile Glu Gly Arg Thr Ala Thr Ser 1 5 10 <210> 2112 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2112 Leu Ala Ala Leu Cys Ser Leu Val His Ser 1 5 10 <210> 2113 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2113 Leu Leu Gly Tyr Leu Leu Ser Ala Glu Cys 1 5 10 <210> 2114 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2114 Gly Tyr Leu Leu Ser Ala Glu Cys Thr Val 1 5 10 <210> 2115 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2115 Ala Leu Phe Leu Gly Val Gly Val Arg Ala 1 5 10 <210> 2116 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2116 Ala Leu Phe Leu Gly Val Gly Val Arg Ala 1 5 10 <210> 2117 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2117 Tyr Arg Gly Cys Val Leu Arg Ser Lys Arg 1 5 10 <210> 2118 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2118 Val Val Ile Leu Val His Gly Glu Leu Arg 1 5 10 <210> 2119 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2119 Ile Phe Val Val Val Ile Leu Val His Gly 1 5 10 <210> 2120 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2120 Asn Pro Met Glu His Ala Asn His Met Ala 1 5 10 <210> 2121 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2121 Thr Ala Asn Pro Met Glu His Ala Asn His 1 5 10 <210> 2122 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2122 Ile Ser Asp Phe Tyr Pro Gly Ala Val Thr 1 5 10 <210> 2123 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2123 Ile Ser Asp Phe Tyr Pro Gly Ala Val Thr 1 5 10 <210> 2124 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2124 Ala Trp Lys Ala Asp Ser Ser Pro Val Lys 1 5 10 <210> 2125 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2125 Phe Leu Ile Phe Leu Gly Lys Thr Trp Gly 1 5 10 <210> 2126 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2126 Val Glu Asn Cys Leu Ala Asn Lys Val Asp 1 5 10 <210> 2127 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2127 Leu Leu Leu Val Leu Leu Pro Thr Asp Ala 1 5 10 <210> 2128 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2128 Leu Met Leu Trp Val Ser Gly Ser Ser Gly 1 5 10 <210> 2129 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2129 Leu Met Leu Trp Val Ser Gly Ser Ser Gly 1 5 10 <210> 2130 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2130 Ala Gln Gly Cys His Arg Arg Met Arg Arg 1 5 10 <210> 2131 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2131 Tyr Gln Leu Val Asp Glu Ser Asp Ala Phe 1 5 10 <210> 2132 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2132 Ser Trp Gly Ser Gly Cys Gly Asp Arg Asn 1 5 10 <210> 2133 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2133 Gly Phe Phe Tyr Thr Pro Lys Thr Arg Arg 1 5 10 <210> 2134 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2134 Val Ser Glu Ser Cys Pro Gly Lys Phe Lys 1 5 10 <210> 2135 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2135 Leu Leu Leu Trp Leu Pro Asp Thr Thr Gly 1 5 10 <210> 2136 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2136 Leu Leu Leu Trp Leu Arg Gly Ala Arg Cys 1 5 10 <210> 2137 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2137 Pro Pro Gly Pro Pro Ser Ala Gly Phe Asp 1 5 10 <210> 2138 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2138 Cys Leu Gly Leu Ser Leu Cys Val Gly Ser 1 5 10 <210> 2139 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2139 Leu Ala Leu Phe Val Gly Ala Gly His Ala 1 5 10 <210> 2140 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2140 Leu Ala Leu Phe Val Gly Ala Gly His Ala 1 5 10 <210> 2141 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2141 His Pro Ala His His Lys Arg Asp Arg Arg 1 5 10 <210> 2142 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2142 Leu Gly Leu Cys Ile Phe Leu Leu Tyr Lys 1 5 10 <210> 2143 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2143 Leu Leu Ala His Cys Thr Gly Ser Trp Ala 1 5 10 <210> 2144 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2144 Leu Ala His Cys Thr Gly Ser Trp Ala Asn 1 5 10 <210> 2145 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2145 Leu Leu Leu Trp Leu Pro Asp Thr Thr Gly 1 5 10 <210> 2146 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2146 Gly Val Leu Gln Ala Cys Pro Thr Arg Gly 1 5 10 <210> 2147 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2147 Pro Pro Pro Pro Gly Pro Phe Ala Arg Arg 1 5 10 <210> 2148 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2148 Pro His Pro Thr Ala Arg Pro Trp Arg Ala 1 5 10 <210> 2149 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2149 Leu Leu Thr Gln Gly Thr Gly Ser Trp Ala 1 5 10 <210> 2150 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2150 Gly Thr Gly Ser Trp Ala Gln Ser Ala Leu 1 5 10 <210> 2151 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2151 Ser Cys His Val Gln His Ser Ser Leu Ala 1 5 10 <210> 2152 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2152 Val Ser Pro Lys Lys Ser Thr Val Leu Gln 1 5 10 <210> 2153 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2153 Lys Phe Glu Val Arg Leu Leu Arg Asp Pro 1 5 10 <210> 2154 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2154 Ile Leu Leu Val Ala Leu Gln Ala Gln Ala 1 5 10 <210> 2155 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2155 Pro Thr Leu Asp Ser Val Leu Tyr Asp Asn 1 5 10 <210> 2156 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2156 Leu Ser Leu Phe Leu Ala Val Gly Leu Gly 1 5 10 <210> 2157 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2157 Leu Ala Ala Ile Leu Lys Gly Val Gln Cys 1 5 10 <210> 2158 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2158 Leu Thr Gln Gly Thr Gly Ser Trp Ala Gln 1 5 10 <210> 2159 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2159 Tyr Asp Ala Asp Cys Glu Asp Ile Asp Cys 1 5 10 <210> 2160 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2160 Glu Lys Gly Glu Arg Gly Glu Gln Gly Arg 1 5 10 <210> 2161 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2161 Gln Pro Leu Gly Met Ile Ser Leu Met Lys 1 5 10 <210> 2162 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2162 Glu Ala Ser Asn Cys Phe Ala Ile Arg His 1 5 10 <210> 2163 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2163 Thr Pro Ser Pro Gly Leu Gln Pro Ala His 1 5 10 <210> 2164 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2164 Gly Glu Glu Pro Ala Arg Arg His Arg Ala 1 5 10 <210> 2165 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2165 Leu Ile Leu Cys Thr Val Ser Val Ala Ser 1 5 10 <210> 2166 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2166 His Pro Ala Leu Asn Gln Pro Gly Gly Leu 1 5 10 <210> 2167 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2167 Lys Glu Pro Val Thr Thr Arg Gln Val Arg 1 5 10 <210> 2168 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2168 Glu Tyr Pro Asp Arg Ile Met Asn Thr Phe 1 5 10 <210> 2169 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2169 Arg Pro Pro Lys Leu His Pro Gly Leu Arg 1 5 10 <210> 2170 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2170 Leu Leu Leu Trp Ile Ser Gly Ala Tyr Gly 1 5 10 <210> 2171 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2171 Val Pro Ala Leu Phe Cys Arg Ala Gly Gly 1 5 10 <210> 2172 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2172 Lys Glu Lys Lys Ser Ala Lys Lys Pro Ser 1 5 10 <210> 2173 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2173 Ile Ser Lys Pro Pro Gly Val Ala Leu Pro 1 5 10 <210> 2174 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2174 Ser Thr Gly Pro Ser Ala Asn Lys Pro Cys 1 5 10 <210> 2175 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2175 Val Gln Cys Ser Asp Leu Gly Leu Asp Lys 1 5 10 <210> 2176 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2176 Arg Leu Glu Ala Gly Asp His Pro Val Glu 1 5 10 <210> 2177 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2177 Pro Gln Pro Gly Val Pro Leu Gly Tyr Pro 1 5 10 <210> 2178 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2178 Gly Gly Pro Gly Phe Gly Pro Gly Val Val 1 5 10 <210> 2179 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2179 Gly Ser Pro Gly Lys Asp Gly Val Arg Gly 1 5 10 <210> 2180 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2180 Glu Pro Gly Pro Ala Gly Ser Asp Gly Leu 1 5 10 <210> 2181 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2181 Leu Asn Arg Lys Tyr Glu Gln Ala Lys Asn 1 5 10 <210> 2182 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2182 Arg Leu Arg Ser Ser Val Pro Gly Val Arg 1 5 10 <210> 2183 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2183 Thr Gly Pro Pro Gly Pro Gln Gly Leu Gln 1 5 10 <210> 2184 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2184 Leu Pro Gly Met Lys Gly Asp Pro Gly Glu 1 5 10 <210> 2185 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2185 Leu Pro Gly Ser Pro Gly Pro Pro Gly Pro 1 5 10 <210> 2186 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2186 Gly Pro Pro Gly Pro Pro Gly Arg Leu Val 1 5 10 <210> 2187 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2187 Val Gly Thr Ala Trp Thr Ala Asp Ser Gly 1 5 10 <210> 2188 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2188 Leu Ser Val Val Gly Thr Ala Trp Thr Ala 1 5 10 <210> 2189 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2189 Val Pro Gly Val Gly Ile Ser Pro Glu Ala 1 5 10 <210> 2190 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2190 His Ala Phe Gly Gln Thr Asp Met Ser Arg 1 5 10 <210> 2191 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2191 Gly Val Ala Pro Gly Ile Gly Pro Gly Gly 1 5 10 <210> 2192 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2192 Ala Pro Arg Gly Val Lys Gly Ala Lys Gly 1 5 10 <210> 2193 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2193 Gly Pro Pro Gly Lys Arg Gly Pro Ser Gly 1 5 10 <210> 2194 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2194 Leu Asn Val Thr Leu Ser Ser Thr Gly Arg 1 5 10 <210> 2195 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2195 Leu Asp Val Ser Leu Gln Leu Pro Ser Arg 1 5 10 <210> 2196 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2196 Asn Arg Gly Asp Ser Thr Phe Glu Ser Lys 1 5 10 <210> 2197 <211> 11 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2197 Val Glu Lys Thr Arg Cys Gln His Glu Arg Glu 1 5 10 <210> 2198 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2198 Gly Pro Lys Gly Gly Ile Gly Asn Arg Gly 1 5 10 <210> 2199 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2199 Arg Pro Pro Gly Phe Ser Pro Phe 1 5 <210> 2200 <211> 9 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2200 Ser His Ala Leu Gln Leu Asn Asn Arg 1 5 <210> 2201 <211> 9 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2201 Arg Pro Pro Gly Phe Ser Pro Phe Arg 1 5 <210> 2202 <211> 9 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2202 His Trp Glu Ser Ala Ser Leu Leu Arg 1 5 <210> 2203 <211> 9 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2203 Thr His Arg Ile His Trp Glu Ser Ala 1 5 <210> 2204 <211> 9 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2204 Leu Gln Leu Asn Asn Arg Gln Ile Arg 1 5 <210> 2205 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2205 Ile His Trp Glu Ser Ala Ser Leu Leu Arg 1 5 10 <210> 2206 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2206 Ala Leu Gln Leu Asn Asn Arg Gln Ile Arg 1 5 10 <210> 2207 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2207 Ile Thr His Arg Ile His Trp Glu Ser Ala 1 5 10 <210> 2208 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2208 Met Glu Pro Leu Gly Arg Gln Leu Thr Ser Gly Pro 1 5 10 <210> 2209 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2209 Arg His Asp Trp Gly His Glu Lys Gln Arg 1 5 10 <210> 2210 <211> 11 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2210 Arg Ile His Trp Glu Ser Ala Ser Leu Leu Arg 1 5 10 <210> 2211 <211> 11 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2211 Lys Ile Thr His Arg Ile His Trp Glu Ser Ala 1 5 10 <210> 2212 <211> 13 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2212 Gly Leu Glu Glu Glu Leu Gln Phe Ser Leu Gly Ser Lys 1 5 10 <210> 2213 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2213 Ser His Ala Leu Gln Leu Asn Asn Arg Gln Ile Arg 1 5 10 <210> 2214 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2214 Ser Lys Ile Thr His Arg Ile His Trp Glu Ser Ala 1 5 10 <210> 2215 <211> 13 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2215 Asn Gly Phe Lys Ser His Ala Leu Gln Leu Asn Asn Arg 1 5 10 <210> 2216 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2216 Arg Pro His Phe Phe Phe Pro Lys Ser Arg Ile Val 1 5 10 <210> 2217 <211> 25 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2217 Ser Ser Ser Tyr Ser Lys Gln Phe Thr Ser Ser Thr Ser Tyr Asn Arg 1 5 10 15 Gly Asp Ser Thr Phe Glu Ser Lys Ser 20 25 <210> 2218 <211> 26 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2218 Ser Ser Ser Tyr Ser Lys Gln Phe Thr Ser Ser Thr Ser Tyr Asn Arg 1 5 10 15 Gly Asp Ser Thr Phe Glu Ser Lys Ser Tyr 20 25 <210> 2219 <211> 64 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2219 His Arg His Pro Asp Glu Ala Ala Phe Phe Asp Thr Ala Ser Thr Gly 1 5 10 15 Lys Thr Phe Pro Gly Phe Phe Ser Pro Met Leu Gly Glu Phe Val Ser 20 25 30 Glu Thr Glu Ser Arg Gly Ser Glu Ser Gly Ile Phe Thr Asn Thr Lys 35 40 45 Glu Ser Ser Ser His Pro Gly Ile Ala Glu Phe Pro Ser Arg Gly 50 55 60 <210> 2220 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2220 Ser Ser Ser Tyr Ser Lys Gln Phe Thr Ser Ser Thr Ser Tyr Asn Arg 1 5 10 15 Gly Asp Ser Thr Phe Glu Ser Lys Ser Tyr Lys Met 20 25 <210> 2221 <211> 16 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2221 Ala Asp Ser Gly Glu Gly Asp Phe Leu Ala Glu Gly Gly Gly Val Arg 1 5 10 15 <210> 2222 <211> 15 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2222 Asp Ser Gly Glu Gly Asp Phe Leu Ala Glu Gly Gly Gly Val Arg 1 5 10 15 <210> 2223 <211> 14 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2223 Asp Ser Gly Glu Gly Asp Phe Leu Ala Glu Gly Gly Gly Val 1 5 10 <210> 2224 <211> 23 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2224 Asp Ser His Ser Leu Thr Thr Asn Ile Met Glu Ile Leu Arg Gly Asp 1 5 10 15 Phe Ser Ser Ala Asn Asn Arg 20 <210> 2225 <211> 14 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2225 Ser Gly Glu Gly Asp Phe Leu Ala Glu Gly Gly Gly Val Arg 1 5 10 <210> 2226 <211> 29 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2226 Ser Ser Ser Tyr Ser Lys Gln Phe Thr Ser Ser Thr Ser Tyr Asn Arg 1 5 10 15 Gly Asp Ser Thr Phe Glu Ser Lys Ser Tyr Lys Met Ala 20 25 <210> 2227 <211> 15 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2227 Ala Asp Ser Gly Glu Gly Asp Phe Leu Ala Glu Gly Gly Gly Val 1 5 10 15 <210> 2228 <211> 22 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2228 Ser Gln Leu Gln Lys Val Pro Pro Glu Trp Lys Ala Leu Thr Asp Met 1 5 10 15 Pro Gln Met Arg Met Glu 20 <210> 2229 <211> 13 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2229 Gly Glu Gly Asp Phe Leu Ala Glu Gly Gly Gly Val Arg 1 5 10 <210> 2230 <211> 26 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2230 Gly Ser Thr Gly Asn Arg Asn Pro Gly Ser Ser Gly Thr Gly Gly Thr 1 5 10 15 Ala Thr Trp Lys Pro Gly Ser Ser Gly Pro 20 25 <210> 2231 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2231 Glu Gly Asp Phe Leu Ala Glu Gly Gly Gly Val Arg 1 5 10 <210> 2232 <211> 29 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2232 Ser Ser Ser Tyr Ser Lys Gln Phe Thr Ser Ser Thr Ser Tyr Asn Arg 1 5 10 15 Gly Asp Ser Thr Phe Glu Ser Lys Ser Tyr Lys Met Ala 20 25 <210> 2233 <211> 23 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2233 Ser Ser Ser Tyr Ser Lys Gln Phe Thr Ser Ser Thr Ser Tyr Asn Arg 1 5 10 15 Gly Asp Ser Thr Phe Glu Ser 20 <210> 2234 <211> 21 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2234 Ala Asp Ser Gly Glu Gly Asp Phe Leu Ala Glu Gly Gly Gly Val Arg 1 5 10 15 Gly Pro Arg Val Val 20 <210> 2235 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2235 Gln Leu Gln Lys Val Pro Pro Glu Trp Lys 1 5 10 <210> 2236 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2236 Val Pro Asp Leu Val Pro Gly Asn Phe Lys 1 5 10 <210> 2237 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2237 Asp Phe Leu Ala Glu Gly Gly Gly Val Arg 1 5 10 <210> 2238 <211> 20 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2238 Ala Asp Ser Gly Glu Gly Asp Phe Leu Ala Glu Gly Gly Gly Val Arg 1 5 10 15 Gly Pro Arg Val 20 <210> 2239 <211> 47 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2239 Thr Phe Pro Gly Phe Phe Ser Pro Met Leu Gly Glu Phe Val Ser Glu 1 5 10 15 Thr Glu Ser Arg Gly Ser Glu Ser Gly Ile Phe Thr Asn Thr Lys Glu 20 25 30 Ser Ser Ser His His Pro Gly Ile Ala Glu Phe Pro Ser Arg Gly 35 40 45 <210> 2240 <211> 13 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2240 Met Lys Pro Val Pro Asp Leu Val Pro Gly Asn Phe Lys 1 5 10 <210> 2241 <211> 17 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2241 Met Lys Pro Val Pro Asp Leu Val Pro Gly Asn Phe Lys Ser Gln Leu 1 5 10 15 Gln <210> 2242 <211> 32 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2242 Ser Gly Ser Ser Gly Pro Gly Ser Thr Gly Asn Arg Asn Pro Gly Ser 1 5 10 15 Ser Gly Thr Gly Gly Thr Ala Thr Trp Lys Pro Gly Ser Ser Gly Pro 20 25 30 <210> 2243 <211> 35 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2243 Met Lys Pro Val Pro Asp Leu Val Pro Gly Asn Phe Lys Ser Gln Leu 1 5 10 15 Gln Lys Val Pro Pro Glu Trp Lys Ala Leu Thr Asp Met Pro Gln Met 20 25 30 Arg Met Glu 35 <210> 2244 <211> 33 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2244 Ser Glu Thr Glu Ser Arg Gly Ser Glu Ser Gly Ile Phe Thr Asn Thr 1 5 10 15 Lys Glu Ser Ser Ser His Pro Gly Ile Ala Glu Phe Pro Ser Arg 20 25 30 Gly <210> 2245 <211> 20 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2245 Asp Ser Gly Glu Gly Asp Phe Leu Ala Glu Gly Gly Gly Val Arg Gly 1 5 10 15 Pro Arg Val Val 20 <210> 2246 <211> 22 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2246 Asp Ser His Ser Leu Thr Thr Asn Ile Met Glu Ile Leu Arg Gly Asp 1 5 10 15 Phe Ser Ser Ala Asn Asn 20 <210> 2247 <211> 22 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2247 Ala Asp Ser Gly Glu Gly Asp Phe Leu Ala Glu Gly Gly Gly Val Arg 1 5 10 15 Gly Pro Arg Val Val Glu 20 <210> 2248 <211> 27 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2248 Met Lys Pro Val Pro Asp Leu Val Pro Gly Asn Phe Lys Ser Gln Leu 1 5 10 15 Gln Lys Val Pro Pro Glu Trp Lys Ala Leu Thr 20 25 <210> 2249 <211> 26 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2249 Ser Glu Ser Gly Ser Phe Arg Pro Asp Ser Pro Gly Ser Gly Asn Ala 1 5 10 15 Arg Pro Asn Asn Pro Asp Trp Gly Thr Phe 20 25 <210> 2250 <211> 9 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2250 Val Pro Asp Leu Val Pro Gly Asn Phe 1 5 <210> 2251 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2251 Leu Glu Arg Pro Gly Gly Asn Glu Ile Thr Arg Gly Gly Ser Thr Ser 1 5 10 15 Tyr Gly Thr Gly Ser Glu Thr Glu Ser Pro Arg Asn 20 25 <210> 2252 <211> 7 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2252 Asp Leu Val Pro Gly Asn Phe 1 5 <210> 2253 <211> 33 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2253 Met Lys Pro Val Pro Asp Leu Val Pro Gly Asn Phe Lys Ser Gln Leu 1 5 10 15 Gln Lys Val Pro Pro Glu Trp Lys Ala Leu Thr Asp Met Pro Gln Met 20 25 30 Arg <210> 2254 <211> 25 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2254 Ala Asp Ser Gly Glu Gly Asp Phe Leu Ala Glu Gly Gly Gly Val Arg 1 5 10 15 Gly Pro Arg Val Val Glu Arg His Gln 20 25 <210> 2255 <211> 14 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2255 Ser Gln Leu Gln Lys Val Pro Pro Glu Trp Lys Ala Leu Thr 1 5 10 <210> 2256 <211> 22 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2256 Ser Ser Tyr Ser Lys Gln Phe Thr Ser Ser Thr Ser Tyr Asn Arg Gly 1 5 10 15 Asp Ser Thr Phe Glu Ser 20 <210> 2257 <211> 35 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2257 Phe Val Ser Glu Thr Glu Ser Arg Gly Ser Glu Ser Gly Ile Phe Thr 1 5 10 15 Asn Thr Lys Glu Ser Ser Ser His His Pro Gly Ile Ala Glu Phe Pro 20 25 30 Ser Arg Gly 35 <210> 2258 <211> 49 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2258 Leu Glu Arg Pro Gly Gly Asn Glu Ile Thr Arg Gly Gly Ser Thr Ser 1 5 10 15 Tyr Gly Thr Gly Ser Glu Thr Glu Ser Pro Arg Asn Pro Ser Ser Ala 20 25 30 Gly Ser Trp Asn Ser Gly Ser Ser Gly Pro Gly Ser Thr Gly Asn Arg 35 40 45 Asn <210> 2259 <211> 20 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2259 Gln Phe Thr Ser Ser Thr Ser Tyr Asn Arg Gly Asp Ser Thr Phe Glu 1 5 10 15 Ser Lys Ser Tyr 20 <210> 2260 <211> 34 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2260 Ser Gly Ser Thr Gly Gln Trp His Ser Glu Ser Gly Ser Phe Arg Pro 1 5 10 15 Asp Ser Pro Gly Ser Gly Asn Ala Arg Pro Asn Asn Pro Asp Trp Gly 20 25 30 Thr Phe <210> 2261 <211> 64 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2261 His Arg His Pro Asp Glu Ala Ala Phe Phe Asp Thr Ala Ser Thr Gly 1 5 10 15 Lys Thr Phe Pro Gly Phe Phe Ser Pro Met Leu Gly Glu Phe Val Ser 20 25 30 Glu Thr Glu Ser Arg Gly Ser Glu Ser Gly Ile Phe Thr Asn Thr Lys 35 40 45 Glu Ser Ser Ser His Pro Gly Ile Ala Glu Phe Pro Ser Arg Gly 50 55 60 <210> 2262 <211> 37 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2262 Met Lys Pro Val Pro Asp Leu Val Pro Gly Asn Phe Lys Ser Gln Leu 1 5 10 15 Gln Lys Val Pro Pro Glu Trp Lys Ala Leu Thr Asp Met Pro Gln Met 20 25 30 Arg Met Glu Leu Glu 35 <210> 2263 <211> 23 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2263 Glu Glu Val Ser Gly Asn Val Ser Pro Gly Thr Arg Arg Glu Tyr His 1 5 10 15 Thr Glu Lys Leu Val Thr Ser 20 <210> 2264 <211> 36 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2264 Leu Glu Arg Pro Gly Gly Asn Glu Ile Thr Arg Gly Gly Ser Thr Ser 1 5 10 15 Tyr Gly Thr Gly Ser Glu Thr Glu Ser Pro Arg Asn Pro Ser Ser Ala 20 25 30 Gly Ser Trp Asn 35 <210> 2265 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2265 Phe Asp Thr Ala Ser Thr Gly Lys Thr Phe Pro Gly 1 5 10 <210> 2266 <211> 49 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2266 Ser Ser Ser Tyr Ser Lys Gln Phe Thr Ser Ser Thr Ser Tyr Asn Arg 1 5 10 15 Gly Asp Ser Thr Phe Glu Ser Lys Ser Tyr Lys Met Ala Asp Glu Ala 20 25 30 Gly Ser Glu Ala Asp His Glu Gly Thr His Ser Thr Lys Arg Gly His 35 40 45 Ala <210> 2267 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2267 Met Lys Pro Val Pro Asp Leu Val Pro Gly Asn Phe 1 5 10 <210> 2268 <211> 39 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2268 Asp Ala Ala Gln Lys Thr Asp Thr Ser His His Asp Gln Asp His Pro 1 5 10 15 Thr Phe Asn Lys Ile Thr Pro Asn Leu Ala Glu Phe Ala Phe Ser Leu 20 25 30 Tyr Arg Gln Leu Ala His Gln 35 <210> 2269 <211> 44 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2269 Glu Asp Pro Gln Gly Asp Ala Ala Gln Lys Thr Asp Thr Ser His His 1 5 10 15 Asp Gln Asp His Pro Thr Phe Asn Lys Ile Thr Pro Asn Leu Ala Glu 20 25 30 Phe Ala Phe Ser Leu Tyr Arg Gln Leu Ala His Gln 35 40 <210> 2270 <211> 40 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2270 Asp Ala Ala Gln Lys Thr Asp Thr Ser His His Asp Gln Asp His Pro 1 5 10 15 Thr Phe Asn Lys Ile Thr Pro Asn Leu Ala Glu Phe Ala Phe Ser Leu 20 25 30 Tyr Arg Gln Leu Ala His Gln Ser 35 40 <210> 2271 <211> 45 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2271 Glu Asp Pro Gln Gly Asp Ala Ala Gln Lys Thr Asp Thr Ser His His 1 5 10 15 Asp Gln Asp His Pro Thr Phe Asn Lys Ile Thr Pro Asn Leu Ala Glu 20 25 30 Phe Ala Phe Ser Leu Tyr Arg Gln Leu Ala His Gln Ser 35 40 45 <210> 2272 <211> 43 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2272 Glu Asp Pro Gln Gly Asp Ala Ala Gln Lys Thr Asp Thr Ser His His 1 5 10 15 Asp Gln Asp His Pro Thr Phe Asn Lys Ile Thr Pro Asn Leu Ala Glu 20 25 30 Phe Ala Phe Ser Leu Tyr Arg Gln Leu Ala His 35 40 <210> 2273 <211> 38 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2273 Asp Ala Ala Gln Lys Thr Asp Thr Ser His His Asp Gln Asp His Pro 1 5 10 15 Thr Phe Asn Lys Ile Thr Pro Asn Leu Ala Glu Phe Ala Phe Ser Leu 20 25 30 Tyr Arg Gln Leu Ala His 35 <210> 2274 <211> 42 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2274 Glu Asp Pro Gln Gly Asp Ala Ala Gln Lys Thr Asp Thr Ser His His 1 5 10 15 Asp Gln Asp His Pro Thr Phe Asn Lys Ile Thr Pro Asn Leu Ala Glu 20 25 30 Phe Ala Phe Ser Leu Tyr Arg Gln Leu Ala 35 40 <210> 2275 <211> 42 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2275 Pro Gln Gly Asp Ala Ala Gln Lys Thr Asp Thr Ser His His Asp Gln 1 5 10 15 Asp His Pro Thr Phe Asn Lys Ile Thr Pro Asn Leu Ala Glu Phe Ala 20 25 30 Phe Ser Leu Tyr Arg Gln Leu Ala His Gln 35 40 <210> 2276 <211> 34 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2276 Lys Pro Arg Leu Leu Leu Phe Ser Pro Ser Val Val His Leu Gly Val 1 5 10 15 Pro Leu Ser Val Gly Val Gln Leu Gln Asp Val Pro Arg Gly Gln Val 20 25 30 Val Lys <210> 2277 <211> 30 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2277 Lys Pro Arg Leu Leu Leu Phe Ser Pro Ser Val Val His Leu Gly Val 1 5 10 15 Pro Leu Ser Val Gly Val Gln Leu Gln Asp Val Pro Arg Gly 20 25 30 <210> 2278 <211> 45 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2278 Lys Pro Arg Leu Leu Leu Phe Ser Pro Ser Val Val His Leu Gly Val 1 5 10 15 Pro Leu Ser Val Gly Val Gln Leu Gln Asp Val Pro Arg Gly Gln Val 20 25 30 Val Lys Gly Ser Val Phe Leu Arg Asn Pro Ser Arg Asn 35 40 45 <210> 2279 <211> 46 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2279 Lys Pro Arg Leu Leu Leu Phe Ser Pro Ser Val Val His Leu Gly Val 1 5 10 15 Pro Leu Ser Val Gly Val Gln Leu Gln Asp Val Pro Arg Gly Gln Val 20 25 30 Val Lys Gly Ser Val Phe Leu Arg Asn Pro Ser Arg Asn Asn 35 40 45 <210> 2280 <211> 19 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2280 Lys Pro Arg Leu Leu Leu Phe Ser Pro Ser Val Val His Leu Gly Val 1 5 10 15 Pro Leu Ser <210> 2281 <211> 38 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2281 Lys Pro Arg Leu Leu Leu Phe Ser Pro Ser Val Val His Leu Gly Val 1 5 10 15 Pro Leu Ser Val Gly Val Gln Leu Gln Asp Val Pro Arg Gly Gln Val 20 25 30 Val Lys Gly Ser Val Phe 35 <210> 2282 <211> 25 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2282 Lys Pro Arg Leu Leu Leu Phe Ser Pro Ser Val Val His Leu Gly Val 1 5 10 15 Pro Leu Ser Val Gly Val Gln Leu Gln 20 25 <210> 2283 <211> 23 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2283 Lys Pro Arg Leu Leu Leu Phe Ser Pro Ser Val Val His Leu Gly Val 1 5 10 15 Pro Leu Ser Val Gly Val Gln 20 <210> 2284 <211> 15 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2284 Asn Gly Phe Lys Ser His Ala Leu Gln Leu Asn Asn Arg Gln Ile 1 5 10 15 <210> 2285 <211> 15 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2285 Lys Pro Arg Leu Leu Leu Phe Ser Pro Ser Val Val His Leu Gly 1 5 10 15 <210> 2286 <211> 16 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2286 Asn Gly Phe Lys Ser His Ala Leu Gln Leu Asn Asn Arg Gln Ile Arg 1 5 10 15 <210> 2287 <211> 21 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2287 Asp Asp Pro Asp Ala Pro Leu Gln Pro Val Thr Pro Leu Gln Leu Phe 1 5 10 15 Glu Gly Arg Arg Asn 20 <210> 2288 <211> 13 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2288 Lys Pro Arg Leu Leu Leu Phe Ser Pro Ser Val Val His 1 5 10 <210> 2289 <211> 17 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2289 Gly Leu Glu Glu Glu Leu Gln Phe Ser Leu Gly Ser Lys Ile Asn Val 1 5 10 15 Lys <210> 2290 <211> 11 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2290 Asp Pro Asp Ala Pro Leu Gln Pro Val Thr Pro 1 5 10 <210> 2291 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2291 Asp Asp Pro Asp Ala Pro Leu Gln Pro Val Thr Pro 1 5 10 <210> 2292 <211> 14 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2292 Gly Phe Lys Ser His Ala Leu Gln Leu Asn Asn Arg Gln Ile 1 5 10 <210> 2293 <211> 14 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2293 Asp Asp Pro Asp Ala Pro Leu Gln Pro Val Thr Pro Leu Gln 1 5 10 <210> 2294 <211> 40 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2294 Lys Pro Arg Leu Leu Leu Phe Ser Pro Ser Val Val His Leu Gly Val 1 5 10 15 Pro Leu Ser Val Gly Val Gln Leu Gln Asp Val Pro Arg Gly Gln Val 20 25 30 Val Lys Gly Ser Val Phe Leu Arg 35 40 <210> 2295 <211> 15 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2295 Asp Asp Pro Asp Ala Pro Leu Gln Pro Val Thr Pro Leu Gln Leu 1 5 10 15 <210> 2296 <211> 13 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2296 Gly Leu Glu Glu Glu Leu Gln Phe Ser Leu Gly Ser Lys 1 5 10 <210> 2297 <211> 25 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2297 Thr Leu Glu Ile Pro Gly Asn Ser Asp Pro Asn Met Ile Pro Asp Gly 1 5 10 15 Asp Phe Asn Ser Tyr Val Arg Val Thr 20 25 <210> 2298 <211> 18 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2298 Leu Phe Ser Pro Ser Val Val His Leu Gly Val Pro Leu Ser Val Gly 1 5 10 15 Val Gln <210> 2299 <211> 16 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2299 Leu Ser Val Ser Ala Gly Ser Pro His Pro Ala Ile Ala Arg Leu Thr 1 5 10 15 <210> 2300 <211> 25 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2300 Val Ala Ala Pro Pro Ser Gly Gly Pro Gly Phe Leu Ser Ile Glu Arg 1 5 10 15 Pro Asp Ser Arg Pro Pro Arg Val Gly 20 25 <210> 2301 <211> 14 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2301 Leu Phe Ser Pro Ser Val Val His Leu Gly Val Pro Leu Ser 1 5 10 <210> 2302 <211> 19 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2302 Pro Asp Ala Pro Leu Gln Pro Val Thr Pro Leu Gln Leu Phe Glu Gly 1 5 10 15 Arg Arg Asn <210> 2303 <211> 20 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2303 Asp Pro Asp Ala Pro Leu Gln Pro Val Thr Pro Leu Gln Leu Phe Glu 1 5 10 15 Gly Arg Arg Asn 20 <210> 2304 <211> 13 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2304 Phe Ser Pro Ser Val Val His Leu Gly Val Pro Leu Ser 1 5 10 <210> 2305 <211> 27 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2305 Asp Glu Leu Pro Ala Lys Asp Asp Pro Asp Ala Pro Leu Gln Pro Val 1 5 10 15 Thr Pro Leu Gln Leu Phe Glu Gly Arg Arg Asn 20 25 <210> 2306 <211> 29 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2306 Leu Phe Ser Pro Ser Val Val His Leu Gly Val Pro Leu Ser Val Gly 1 5 10 15 Val Gln Leu Gln Asp Val Pro Arg Gly Gln Val Val Lys 20 25 <210> 2307 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2307 Leu Phe Ser Pro Ser Val Val His Leu Gly 1 5 10 <210> 2308 <211> 23 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2308 Ala Pro Pro Ser Gly Gly Pro Gly Phe Leu Ser Ile Glu Arg Pro Asp 1 5 10 15 Ser Arg Pro Pro Arg Val Gly 20 <210> 2309 <211> 18 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2309 Glu Glu Ala Pro Ser Leu Arg Pro Ala Pro Pro Pro Ile Ser Gly Gly 1 5 10 15 Gly Tyr <210> 2310 <211> 17 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2310 Glu Ala Pro Ser Leu Arg Pro Ala Pro Pro Pro Ile Ser Gly Gly Gly 1 5 10 15 Tyr <210> 2311 <211> 19 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2311 Arg Glu Glu Ala Pro Ser Leu Arg Pro Ala Pro Pro Pro Ile Ser Gly 1 5 10 15 Gly Gly Tyr <210> 2312 <211> 41 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2312 Gln Gly Val Asn Asp Asn Glu Glu Gly Phe Phe Ser Ala Arg Gly His 1 5 10 15 Arg Pro Leu Asp Lys Lys Arg Glu Glu Ala Pro Ser Leu Arg Pro Ala 20 25 30 Pro Pro Pro Ile Ser Gly Gly Gly Tyr 35 40 <210> 2313 <211> 14 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2313 Gln Gly Val Asn Asp Asn Glu Glu Gly Phe Phe Ser Ala Arg 1 5 10 <210> 2314 <211> 16 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2314 Gln Gly Val Asn Asp Asn Glu Glu Gly Phe Phe Ser Ala Arg Gly His 1 5 10 15 <210> 2315 <211> 13 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2315 Gln Gly Val Asn Asp Asn Glu Glu Gly Phe Phe Ser Ala 1 5 10 <210> 2316 <211> 24 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2316 Gln Gly Val Asn Asp Asn Glu Glu Gly Phe Phe Ser Ala Arg Gly His 1 5 10 15 Arg Pro Leu Asp Lys Lys Arg Glu 20 <210> 2317 <211> 20 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2317 Lys Arg Glu Glu Ala Pro Ser Leu Arg Pro Ala Pro Pro Pro Ile Ser 1 5 10 15 Gly Gly Gly Tyr 20 <210> 2318 <211> 42 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2318 Gln Gly Val Asn Asp Asn Glu Glu Gly Phe Phe Ser Ala Arg Gly His 1 5 10 15 Arg Pro Leu Asp Lys Lys Arg Glu Glu Ala Pro Ser Leu Arg Pro Ala 20 25 30 Pro Pro Pro Ile Ser Gly Gly Gly Tyr Arg 35 40 <210> 2319 <211> 20 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2319 Gln Gly Val Asn Asp Asn Glu Glu Gly Phe Phe Ser Ala Arg Gly His 1 5 10 15 Arg Pro Leu Asp 20 <210> 2320 <211> 22 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2320 Asp Lys Lys Arg Glu Glu Ala Pro Ser Leu Arg Pro Ala Pro Pro Pro 1 5 10 15 Ile Ser Gly Gly Gly Tyr 20 <210> 2321 <211> 23 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2321 Gln Gly Val Asn Asp Asn Glu Glu Gly Phe Phe Ser Ala Arg Gly His 1 5 10 15 Arg Pro Leu Asp Lys Lys Arg 20 <210> 2322 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2322 Asn Asp Asn Glu Glu Gly Phe Phe Ser Ala 1 5 10 <210> 2323 <211> 47 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2323 Gln Gly Val Asn Asp Asn Glu Glu Gly Phe Phe Ser Ala Arg Gly His 1 5 10 15 Arg Pro Leu Asp Lys Lys Arg Glu Glu Ala Pro Ser Leu Arg Pro Ala 20 25 30 Pro Pro Pro Ile Ser Gly Gly Gly Tyr Arg Ala Arg Pro Ala Lys 35 40 45 <210> 2324 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2324 Gln Gly Val Asn Asp Asn Glu Glu Gly Phe Phe Ser 1 5 10 <210> 2325 <211> 18 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2325 Val Asn Asp Asn Glu Glu Gly Phe Phe Ser Ala Arg Gly His Arg Pro 1 5 10 15 Leu Asp <210> 2326 <211> 40 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2326 Val Asn Asp Asn Glu Glu Gly Phe Phe Ser Ala Arg Gly His Arg Pro 1 5 10 15 Leu Asp Lys Lys Arg Glu Glu Ala Pro Ser Leu Arg Pro Ala Pro Pro 20 25 30 Pro Ile Ser Gly Gly Gly Tyr Arg 35 40 <210> 2327 <211> 19 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2327 Val Asn Asp Asn Glu Glu Gly Phe Phe Ser Ala Arg Gly His Arg Pro 1 5 10 15 Leu Asp Lys <210> 2328 <211> 29 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2328 Gln Gly Val Asn Asp Asn Glu Glu Gly Phe Phe Ser Ala Arg Gly His 1 5 10 15 Arg Pro Leu Asp Lys Lys Arg Glu Glu Ala Pro Ser Leu 20 25 <210> 2329 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2329 Gln Gly Val Asn Asp Asn Glu Glu Gly Phe Phe Ser Ala Arg Gly His 1 5 10 15 Arg Pro Leu Asp Lys Lys Arg Glu Glu Ala Pro Ser 20 25 <210> 2330 <211> 22 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2330 Gln Gly Val Asn Asp Asn Glu Glu Gly Phe Phe Ser Ala Arg Gly His 1 5 10 15 Arg Pro Leu Asp Lys Lys 20 <210> 2331 <211> 11 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2331 Val Asn Asp Asn Glu Glu Gly Phe Phe Ser Ala 1 5 10 <210> 2332 <211> 21 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2332 Lys Arg Glu Glu Ala Pro Ser Leu Arg Pro Ala Pro Pro Pro Ile Ser 1 5 10 15 Gly Gly Gly Tyr Arg 20 <210> 2333 <211> 27 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2333 Gly His Arg Pro Leu Asp Lys Lys Arg Glu Glu Ala Pro Ser Leu Arg 1 5 10 15 Pro Ala Pro Pro Pro Ile Ser Gly Gly Gly Tyr 20 25 <210> 2334 <211> 17 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2334 Asn Asp Asn Glu Glu Gly Phe Phe Ser Ala Arg Gly His Arg Pro Leu 1 5 10 15 Asp <210> 2335 <211> 45 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2335 Gln Gly Val Asn Asp Asn Glu Glu Gly Phe Phe Ser Ala Arg Gly His 1 5 10 15 Arg Pro Leu Asp Lys Lys Arg Glu Glu Ala Pro Ser Leu Arg Pro Ala 20 25 30 Pro Pro Pro Ile Ser Gly Gly Gly Tyr Arg Ala Arg Pro 35 40 45 <210> 2336 <211> 49 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2336 Gln Gly Val Asn Asp Asn Glu Glu Gly Phe Phe Ser Ala Arg Gly His 1 5 10 15 Arg Pro Leu Asp Lys Lys Arg Glu Glu Ala Pro Ser Leu Arg Pro Ala 20 25 30 Pro Pro Pro Ile Ser Gly Gly Gly Tyr Arg Ala Arg Pro Ala Lys Ala 35 40 45 Ala <210> 2337 <211> 9 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2337 Asp Asn Glu Glu Gly Phe Phe Ser Ala 1 5 <210> 2338 <211> 37 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2338 Gln Gly Val Asn Asp Asn Glu Glu Gly Phe Phe Ser Ala Arg Gly His 1 5 10 15 Arg Pro Leu Asp Lys Lys Arg Glu Glu Ala Pro Ser Leu Arg Pro Ala 20 25 30 Pro Pro Pro Ile Ser 35 <210> 2339 <211> 25 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2339 Gln Gly Val Asn Asp Asn Glu Glu Gly Phe Phe Ser Ala Arg Gly His 1 5 10 15 Arg Pro Leu Asp Lys Lys Arg Glu Glu 20 25 <210> 2340 <211> 46 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2340 Gln Gly Val Asn Asp Asn Glu Glu Gly Phe Phe Ser Ala Arg Gly His 1 5 10 15 Arg Pro Leu Asp Lys Lys Arg Glu Glu Ala Pro Ser Leu Arg Pro Ala 20 25 30 Pro Pro Pro Ile Ser Gly Gly Gly Tyr Arg Ala Arg Pro Ala 35 40 45 <210> 2341 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2341 Arg Ser Phe Phe Ser Phe Leu Gly Glu Ala Phe Asp 1 5 10 <210> 2342 <211> 38 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2342 Asp Gly Ala Arg Asp Met Trp Arg Ala Tyr Ser Asp Met Arg Glu Ala 1 5 10 15 Asn Tyr Ile Gly Ser Asp Lys Tyr Phe His Ala Arg Gly Asn Tyr Asp 20 25 30 Ala Ala Lys Arg Gly Pro 35 <210> 2343 <211> 11 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2343 Ser Phe Phe Ser Phe Leu Gly Glu Ala Phe Asp 1 5 10 <210> 2344 <211> 44 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2344 Phe Leu Gly Glu Ala Phe Asp Gly Ala Arg Asp Met Trp Arg Ala Tyr 1 5 10 15 Ser Asp Met Arg Glu Ala Asn Tyr Ile Gly Ser Asp Lys Tyr Phe His 20 25 30 Ala Arg Gly Asn Tyr Asp Ala Ala Lys Arg Gly Pro 35 40 <210> 2345 <211> 36 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2345 Phe Phe Gly His Gly Ala Glu Asp Ser Leu Ala Asp Gln Ala Ala Asn 1 5 10 15 Glu Trp Gly Arg Ser Gly Lys Asp Pro Asn His Phe Arg Pro Ala Gly 20 25 30 Leu Pro Glu Lys 35 <210> 2346 <211> 45 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2346 Ser Phe Leu Gly Glu Ala Phe Asp Gly Ala Arg Asp Met Trp Arg Ala 1 5 10 15 Tyr Ser Asp Met Arg Glu Ala Asn Tyr Ile Gly Ser Asp Lys Tyr Phe 20 25 30 His Ala Arg Gly Asn Tyr Asp Ala Ala Lys Arg Gly Pro 35 40 45 <210> 2347 <211> 20 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2347 Asp Gln Ala Ala Asn Glu Trp Gly Arg Ser Gly Lys Asp Pro Asn His 1 5 10 15 Phe Arg Pro Ala 20 <210> 2348 <211> 15 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2348 Ala Arg Glu Asn Ile Gln Arg Phe Phe Gly His Gly Ala Glu Asp 1 5 10 15 <210> 2349 <211> 42 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2349 Gly Glu Ala Phe Asp Gly Ala Arg Asp Met Trp Arg Ala Tyr Ser Asp 1 5 10 15 Met Arg Glu Ala Asn Tyr Ile Gly Ser Asp Lys Tyr Phe His Ala Arg 20 25 30 Gly Asn Tyr Asp Ala Ala Lys Arg Gly Pro 35 40 <210> 2350 <211> 7 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2350 Arg Ser Phe Phe Ser Phe Leu 1 5 <210> 2351 <211> 26 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2351 Gly Pro Arg Arg Tyr Thr Ile Ala Ala Leu Leu Ser Pro Tyr Ser Tyr 1 5 10 15 Ser Thr Thr Ala Val Val Thr Asn Pro Lys 20 25 <210> 2352 <211> 37 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2352 Met Glu Pro Leu Gly Arg Gln Leu Thr Ser Gly Pro Asn Gln Glu Gln 1 5 10 15 Val Ser Pro Leu Thr Leu Leu Lys Leu Gly Asn Gln Glu Pro Gly Gly 20 25 30 Gln Thr Ala Leu Lys 35 <210> 2353 <211> 24 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2353 Met Glu Pro Leu Gly Arg Gln Leu Thr Ser Gly Pro Asn Gln Glu Gln 1 5 10 15 Val Ser Pro Leu Thr Leu Leu Lys 20 <210> 2354 <211> 25 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2354 Asn Gln Glu Gln Val Ser Pro Leu Thr Leu Leu Lys Leu Gly Asn Gln 1 5 10 15 Glu Pro Gly Gly Gln Thr Ala Leu Lys 20 25 <210> 2355 <211> 15 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2355 Ser Gly Pro Asn Gln Glu Gln Val Ser Pro Leu Thr Leu Leu Lys 1 5 10 15 <210> 2356 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2356 Met Glu Pro Leu Gly Arg Gln Leu Thr Ser Gly Pro 1 5 10 <210> 2357 <211> 11 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2357 Glu Pro Leu Gly Arg Gln Leu Thr Ser Gly Pro 1 5 10 <210> 2358 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2358 Asn Gln Glu Gln Val Ser Pro Leu Thr Leu Leu Lys 1 5 10 <210> 2359 <211> 14 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2359 Asn Gln Glu Gln Val Ser Pro Leu Thr Leu Leu Lys Leu Gly 1 5 10 <210> 2360 <211> 45 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2360 Met Ser Leu Ser Ser Phe Ser Val Asn Arg Pro Phe Leu Phe Phe Ile 1 5 10 15 Phe Glu Asp Thr Thr Gly Leu Pro Leu Phe Val Gly Ser Val Arg Asn 20 25 30 Pro Asn Pro Ser Ala Pro Arg Glu Leu Lys Glu Gln Gln 35 40 45 <210> 2361 <211> 22 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2361 Met Glu Pro Leu Gly Arg Gln Leu Thr Ser Gly Pro Asn Gln Glu Gln 1 5 10 15 Val Ser Pro Leu Thr Leu 20 <210> 2362 <211> 29 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2362 Leu Ala Thr Val Tyr Val Asp Val Leu Lys Asp Ser Gly Arg Asp Tyr 1 5 10 15 Val Ser Gln Phe Glu Gly Ser Ala Leu Gly Lys Gln Leu 20 25 <210> 2363 <211> 23 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2363 Asp Glu Pro Pro Gln Ser Pro Trp Asp Arg Val Lys Asp Leu Ala Thr 1 5 10 15 Val Tyr Val Asp Val Leu Lys 20 <210> 2364 <211> 13 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2364 Asn Leu Glu Lys Glu Thr Glu Gly Leu Arg Gln Glu Met 1 5 10 <210> 2365 <211> 13 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2365 Asp Glu Pro Pro Gln Ser Pro Trp Asp Arg Val Lys Asp 1 5 10 <210> 2366 <211> 15 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2366 Ala Glu Leu Gln Glu Gly Ala Arg Gln Lys Leu His Glu Leu Gln 1 5 10 15 <210> 2367 <211> 22 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2367 Ala Glu Leu Gln Glu Gly Ala Arg Gln Lys Leu His Glu Leu Gln Glu 1 5 10 15 Lys Leu Ser Pro Leu Gly 20 <210> 2368 <211> 18 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2368 Asp Glu Pro Pro Gln Ser Pro Trp Asp Arg Val Lys Asp Leu Ala Thr 1 5 10 15 Val Tyr <210> 2369 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2369 Asn Ser Pro Leu Asp Glu Glu Asn Leu Thr 1 5 10 <210> 2370 <211> 27 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2370 His Pro Asn Ser Pro Leu Asp Glu Glu Asn Leu Thr Gln Glu Asn Gln 1 5 10 15 Asp Arg Gly Thr His Val Asp Leu Gly Leu Ala 20 25 <210> 2371 <211> 30 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2371 Arg Ser Leu Gln Asp Thr Glu Glu Lys Ser Arg Ser Phe Ser Ala Ser 1 5 10 15 Gln Ala Asp Pro Leu Ser Asp Pro Asp Gln Met Asn Glu Asp 20 25 30 <210> 2372 <211> 29 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2372 Arg Ser Leu Gln Asp Thr Glu Glu Lys Ser Arg Ser Phe Ser Ala Ser 1 5 10 15 Gln Ala Asp Pro Leu Ser Asp Pro Asp Gln Met Asn Glu 20 25 <210> 2373 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2373 Leu Gln Asp Thr Glu Glu Lys Ser Arg Ser Phe Ser Ala Ser Gln Ala 1 5 10 15 Asp Pro Leu Ser Asp Pro Asp Gln Met Asn Glu Asp 20 25 <210> 2374 <211> 29 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2374 Ser Leu Gln Asp Thr Glu Glu Lys Ser Arg Ser Phe Ser Ala Ser Gln 1 5 10 15 Ala Asp Pro Leu Ser Asp Pro Asp Gln Met Asn Glu Asp 20 25 <210> 2375 <211> 21 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2375 His Ser Gln Gly Thr Phe Thr Ser Asp Tyr Ser Lys Tyr Leu Asp Ser 1 5 10 15 Arg Arg Ala Gln Asp 20 <210> 2376 <211> 27 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2376 Leu Gln Asp Thr Glu Glu Lys Ser Arg Ser Phe Ser Ala Ser Gln Ala 1 5 10 15 Asp Pro Leu Ser Asp Pro Asp Gln Met Asn Glu 20 25 <210> 2377 <211> 29 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2377 His Ser Gln Gly Thr Phe Thr Ser Asp Tyr Ser Lys Tyr Leu Asp Ser 1 5 10 15 Arg Arg Ala Gln Asp Phe Val Gln Trp Leu Met Asn Thr 20 25 <210> 2378 <211> 27 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2378 Gln Asp Thr Glu Glu Lys Ser Arg Ser Phe Ser Ala Ser Gln Ala Asp 1 5 10 15 Pro Leu Ser Asp Pro Asp Gln Met Asn Glu Asp 20 25 <210> 2379 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2379 Ser Leu Gln Asp Thr Glu Glu Lys Ser Arg Ser Phe Ser Ala Ser Gln 1 5 10 15 Ala Asp Pro Leu Ser Asp Pro Asp Gln Met Asn Glu 20 25 <210> 2380 <211> 48 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2380 Asp Phe Pro Glu Glu Val Ala Ile Val Glu Glu Leu Gly Arg Arg His 1 5 10 15 Ala Asp Gly Ser Phe Ser Asp Glu Met Asn Thr Ile Leu Asp Asn Leu 20 25 30 Ala Ala Arg Asp Phe Ile Asn Trp Leu Ile Gln Thr Lys Ile Thr Asp 35 40 45 <210> 2381 <211> 37 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2381 His Asp Glu Phe Glu Arg His Ala Glu Gly Thr Phe Thr Ser Asp Val 1 5 10 15 Ser Ser Tyr Leu Glu Gly Gln Ala Ala Lys Glu Phe Ile Ala Trp Leu 20 25 30 Val Lys Gly Arg Gly 35 <210> 2382 <211> 30 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2382 Ser Val Phe Pro Gln Gln Thr Gly Gln Leu Ala Glu Leu Gln Pro Gln 1 5 10 15 Asp Arg Ala Gly Ala Arg Ala Ser Trp Met Pro Met Phe Gln 20 25 30 <210> 2383 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2383 Ser Val Phe Pro Gln Gln Thr Gly Gln Leu Ala Glu Leu Gln Pro Gln 1 5 10 15 Asp Arg Ala Gly Ala Arg Ala Ser Trp Met Pro Met 20 25 <210> 2384 <211> 27 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2384 Ser Val Phe Pro Gln Gln Thr Gly Gln Leu Ala Glu Leu Gln Pro Gln 1 5 10 15 Asp Arg Ala Gly Ala Arg Ala Ser Trp Met Pro 20 25 <210> 2385 <211> 23 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2385 Ser Val Phe Pro Gln Gln Thr Gly Gln Leu Ala Glu Leu Gln Pro Gln 1 5 10 15 Asp Arg Ala Gly Ala Arg Ala 20 <210> 2386 <211> 24 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2386 Ser Val Phe Pro Gln Gln Thr Gly Gln Leu Ala Glu Leu Gln Pro Gln 1 5 10 15 Asp Arg Ala Gly Ala Arg Ala Ser 20 <210> 2387 <211> 21 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2387 Ser Val Phe Pro Gln Gln Thr Gly Gln Leu Ala Glu Leu Gln Pro Gln 1 5 10 15 Asp Arg Ala Gly Ala 20 <210> 2388 <211> 20 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2388 Gln Gln Thr Gly Gln Leu Ala Glu Leu Gln Pro Gln Asp Arg Ala Gly 1 5 10 15 Ala Arg Ala Ser 20 <210> 2389 <211> 23 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2389 Val Phe Pro Gln Gln Thr Gly Gln Leu Ala Glu Leu Gln Pro Gln Asp 1 5 10 15 Arg Ala Gly Ala Arg Ala Ser 20 <210> 2390 <211> 17 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2390 Gln Gln Thr Gly Gln Leu Ala Glu Leu Gln Pro Gln Asp Arg Ala Gly 1 5 10 15 Ala <210> 2391 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2391 Ser Val Phe Pro Gln Gln Thr Gly Gln Leu Ala Glu 1 5 10 <210> 2392 <211> 22 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2392 Ser Val Phe Pro Gln Gln Thr Gly Gln Leu Ala Glu Leu Gln Pro Gln 1 5 10 15 Asp Arg Ala Gly Ala Arg 20 <210> 2393 <211> 15 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2393 Ser Val Phe Pro Gln Gln Thr Gly Gln Leu Ala Glu Leu Gln Pro 1 5 10 15 <210> 2394 <211> 26 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2394 Thr Gly Arg Gly Ala Glu Asp Ser Leu Ala Asp Gln Ala Ala Asn Lys 1 5 10 15 Trp Gly Arg Ser Gly Arg Asp Pro Asn His 20 25 <210> 2395 <211> 27 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2395 Leu Thr Gly Arg Gly Ala Glu Asp Ser Leu Ala Asp Gln Ala Ala Asn 1 5 10 15 Lys Trp Gly Arg Ser Gly Arg Asp Pro Asn His 20 25 <210> 2396 <211> 22 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2396 Ala Glu Asp Ser Leu Ala Asp Gln Ala Ala Asn Lys Trp Gly Arg Ser 1 5 10 15 Gly Arg Asp Pro Asn His 20 <210> 2397 <211> 11 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2397 Gly Pro Gly Gly Ala Trp Ala Ala Glu Val Ile 1 5 10 <210> 2398 <211> 17 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2398 Ser Asp Lys Pro Asp Met Ala Glu Ile Glu Lys Phe Asp Lys Ser Lys 1 5 10 15 Leu <210> 2399 <211> 21 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2399 Ser Asp Lys Pro Asp Met Ala Glu Ile Glu Lys Phe Asp Lys Ser Lys 1 5 10 15 Leu Lys Lys Thr Glu 20 <210> 2400 <211> 24 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2400 Ser Asp Lys Pro Asp Met Ala Glu Ile Glu Lys Phe Asp Lys Ser Lys 1 5 10 15 Leu Lys Lys Thr Glu Thr Gln Glu 20 <210> 2401 <211> 21 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2401 Ile Leu Gly Gly His Leu Asp Ala Lys Gly Ser Phe Pro Trp Gln Ala 1 5 10 15 Lys Met Val Ser His 20 <210> 2402 <211> 22 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2402 Ile Leu Gly Gly His Leu Asp Ala Lys Gly Ser Phe Pro Trp Gln Ala 1 5 10 15 Lys Met Val Ser His His 20 <210> 2403 <211> 19 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2403 Ile Leu Gly Gly His Leu Asp Ala Lys Gly Ser Phe Pro Trp Gln Ala 1 5 10 15 Lys Met Val <210> 2404 <211> 15 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2404 Ile Leu Gly Gly His Leu Asp Ala Lys Gly Ser Phe Pro Trp Gln 1 5 10 15 <210> 2405 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2405 Ala Val Ile Ala Leu Leu Leu Trp Gly Gln 1 5 10 <210> 2406 <211> 11 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2406 Gly Ala Val Ile Ala Leu Leu Leu Trp Gly Gln 1 5 10 <210> 2407 <211> 32 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2407 Val Leu Ser Pro Ala Asp Lys Thr Asn Val Lys Ala Ala Trp Gly Lys 1 5 10 15 Val Gly Ala His Ala Gly Glu Tyr Gly Ala Glu Ala Leu Glu Arg Met 20 25 30 <210> 2408 <211> 33 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2408 Val Leu Ser Pro Ala Asp Lys Thr Asn Val Lys Ala Ala Trp Gly Lys 1 5 10 15 Val Gly Ala His Ala Gly Glu Tyr Gly Ala Glu Ala Leu Glu Arg Met 20 25 30 Phe <210> 2409 <211> 36 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2409 Val Leu Ser Pro Ala Asp Lys Thr Asn Val Lys Ala Ala Trp Gly Lys 1 5 10 15 Val Gly Ala His Ala Gly Glu Tyr Gly Ala Glu Ala Leu Glu Arg Met 20 25 30 Phe Leu Ser Phe 35 <210> 2410 <211> 18 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2410 Val Leu Ser Pro Ala Asp Lys Thr Asn Val Lys Ala Ala Trp Gly Lys 1 5 10 15 Val Gly <210> 2411 <211> 18 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2411 Gly Glu Asp Ala Ala Gln Ala Glu Lys Phe Gln His Pro Gly Ser Asp 1 5 10 15 Met Arg <210> 2412 <211> 14 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2412 Gly Glu Asp Ala Ala Gln Ala Glu Lys Phe Gln His Pro Gly 1 5 10 <210> 2413 <211> 17 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2413 Gly Glu Asp Ala Ala Gln Ala Glu Lys Phe Gln His Pro Gly Ser Asp 1 5 10 15 Met <210> 2414 <211> 17 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2414 Ala Pro Gly Leu Pro Pro Ala Gly Ser Pro Pro Asp Ser His Val Leu 1 5 10 15 Leu <210> 2415 <211> 18 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2415 Ala Pro Gly Leu Pro Pro Ala Gly Ser Pro Pro Asp Ser His Val Leu 1 5 10 15 Leu Ala <210> 2416 <211> 38 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2416 Ala Ala Pro Pro Gly His Gln Leu His Arg Ala His Tyr Asp Leu Arg 1 5 10 15 His Thr Phe Met Gly Val Val Ser Leu Gly Ser Pro Ser Gly Glu Val 20 25 30 Ser His Pro Arg Lys Thr 35 <210> 2417 <211> 55 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2417 Ala Pro Gly Leu Pro Pro Ala Gly Ser Pro Pro Asp Ser His Val Leu 1 5 10 15 Leu Ala Ala Pro Pro Gly His Gln Leu His Arg Ala His Tyr Asp Leu 20 25 30 Arg His Thr Phe Met Gly Val Val Ser Leu Gly Ser Pro Ser Gly Glu 35 40 45 Val Ser His Pro Arg Lys Thr 50 55 <210> 2418 <211> 37 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2418 Ala Pro Pro Gly His Gln Leu His Arg Ala His Tyr Asp Leu Arg His 1 5 10 15 Thr Phe Met Gly Val Val Ser Leu Gly Ser Pro Ser Gly Glu Val Ser 20 25 30 His Pro Arg Lys Thr 35 <210> 2419 <211> 16 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2419 Ala Pro Gly Leu Pro Pro Ala Gly Ser Pro Pro Asp Ser His Val Leu 1 5 10 15 <210> 2420 <211> 36 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2420 Ala Ala Pro Pro Gly His Gln Leu His Arg Ala His Tyr Asp Leu Arg 1 5 10 15 His Thr Phe Met Gly Val Val Ser Leu Gly Ser Pro Ser Gly Glu Val 20 25 30 Ser His Pro Arg 35 <210> 2421 <211> 34 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2421 His Ser Gly Phe Glu Asp Glu Leu Ser Glu Val Leu Glu Asn Gln Ser 1 5 10 15 Ser Gln Ala Glu Leu Lys Glu Ala Val Glu Glu Pro Ser Ser Lys Asp 20 25 30 Val Met <210> 2422 <211> 35 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2422 His Ser Gly Phe Glu Asp Glu Leu Ser Glu Val Leu Glu Asn Gln Ser 1 5 10 15 Ser Gln Ala Glu Leu Lys Glu Ala Val Glu Glu Pro Ser Ser Lys Asp 20 25 30 Val Met Glu 35 <210> 2423 <211> 44 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2423 Gly Tyr Pro Glu Glu Lys Lys Glu Glu Glu Gly Ser Ala Asn Arg Arg 1 5 10 15 Pro Glu Asp Gln Glu Leu Glu Ser Leu Ser Ala Ile Glu Ala Glu Leu 20 25 30 Glu Lys Val Ala His Gln Leu Gln Ala Leu Arg Arg 35 40 <210> 2424 <211> 34 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2424 His Ser Gly Phe Glu Asp Glu Leu Ser Glu Val Leu Glu Asn Gln Ser 1 5 10 15 Ser Gln Ala Glu Leu Lys Glu Ala Val Glu Glu Pro Ser Ser Lys Asp 20 25 30 Val Met <210> 2425 <211> 33 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2425 Leu Glu Gly Gln Glu Glu Glu Glu Asp Asn Arg Asp Ser Ser Met Lys 1 5 10 15 Leu Ser Phe Arg Ala Arg Ala Tyr Gly Phe Arg Gly Pro Gly Pro Gln 20 25 30 Leu <210> 2426 <211> 19 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2426 Leu Glu Gly Gln Glu Glu Glu Glu Asp Asn Arg Asp Ser Ser Met Lys 1 5 10 15 Leu Ser Phe <210> 2427 <211> 17 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2427 Ser Ser Lys Ile Thr His Arg Ile His Trp Glu Ser Ala Ser Leu Leu 1 5 10 15 Arg <210> 2428 <211> 16 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2428 Ser Ser Lys Ile Thr His Arg Ile His Trp Glu Ser Ala Ser Leu Leu 1 5 10 15 <210> 2429 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2429 Thr His Arg Ile His Trp Glu Ser Ala Ser Leu Leu 1 5 10 <210> 2430 <211> 14 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2430 Lys Ile Thr His Arg Ile His Trp Glu Ser Ala Ser Leu Leu 1 5 10 <210> 2431 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2431 Ser Pro Met Tyr Ser Ile Ile Thr Pro Asn Ile Leu Arg Leu Glu Ser 1 5 10 15 Glu Glu Thr Met Val Leu Glu Ala His Asp Ala Gln 20 25 <210> 2432 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2432 Arg Ile His Trp Glu Ser Ala Ser Leu Leu 1 5 10 <210> 2433 <211> 11 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2433 His Arg Ile His Trp Glu Ser Ala Ser Leu Leu 1 5 10 <210> 2434 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2434 His Trp Glu Ser Ala Ser Leu Leu 1 5 <210> 2435 <211> 9 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2435 Ile His Trp Glu Ser Ala Ser Leu Leu 1 5 <210> 2436 <211> 42 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2436 Thr Ser Ala Gly Thr Arg Gln Pro Gln Phe Ile Ser Arg Asp Trp His 1 5 10 15 Gly Val Pro Gly Gln Val Asp Ala Ala Met Ala Gly Arg Ile Tyr Ile 20 25 30 Ser Gly Met Ala Pro Arg Pro Ser Leu Ala 35 40 <210> 2437 <211> 29 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2437 Thr Arg Gln Pro Gln Phe Ile Ser Arg Asp Trp His Gly Val Pro Gly 1 5 10 15 Gln Val Asp Ala Ala Met Ala Gly Arg Ile Tyr Ile Ser 20 25 <210> 2438 <211> 33 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2438 Leu Gln Ala Gln Ser Lys Gly Asn Pro Glu Gln Thr Pro Val Leu Lys 1 5 10 15 Pro Glu Glu Glu Ala Pro Ala Pro Glu Val Gly Ala Ser Lys Pro Glu 20 25 30 Gly <210> 2439 <211> 46 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2439 Phe Trp Gly Arg Thr Ser Ala Gly Thr Arg Gln Pro Gln Phe Ile Ser 1 5 10 15 Arg Asp Trp His Gly Val Pro Gly Gln Val Asp Ala Ala Met Ala Gly 20 25 30 Arg Ile Tyr Ile Ser Gly Met Ala Pro Arg Pro Ser Leu Ala 35 40 45 <210> 2440 <211> 35 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2440 Thr Arg Gln Pro Gln Phe Ile Ser Arg Asp Trp His Gly Val Pro Gly 1 5 10 15 Gln Val Asp Ala Ala Met Ala Gly Arg Ile Tyr Ile Ser Gly Met Ala 20 25 30 Pro Arg Pro 35 <210> 2441 <211> 42 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2441 Thr Ser Ala Gly Thr Arg Gln Pro Gln Phe Ile Ser Arg Asp Trp His 1 5 10 15 Gly Val Pro Gly Gln Val Asp Ala Ala Met Ala Gly Arg Ile Tyr Ile 20 25 30 Ser Gly Met Ala Pro Arg Pro Ser Leu Ala 35 40 <210> 2442 <211> 44 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2442 Phe Trp Gly Arg Thr Ser Ala Gly Thr Arg Gln Pro Gln Phe Ile Ser 1 5 10 15 Arg Asp Trp His Gly Val Pro Gly Gln Val Asp Ala Ala Met Ala Gly 20 25 30 Arg Ile Tyr Ile Ser Gly Met Ala Pro Arg Pro Ser 35 40 <210> 2443 <211> 27 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2443 Ser Val Phe Leu Ile Lys Gly Asp Lys Val Trp Val Tyr Pro Pro Glu 1 5 10 15 Lys Lys Glu Lys Gly Tyr Pro Lys Leu Leu Gln 20 25 <210> 2444 <211> 17 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2444 Ser Val Phe Leu Ile Lys Gly Asp Lys Val Trp Val Tyr Pro Pro Glu 1 5 10 15 Lys <210> 2445 <211> 19 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2445 Ser Val Phe Leu Ile Lys Gly Asp Lys Val Trp Val Tyr Pro Pro Glu 1 5 10 15 Lys Lys Glu <210> 2446 <211> 14 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2446 Phe Pro Ser Pro Val Asp Ala Ala Phe Arg Gln Gly His Asn 1 5 10 <210> 2447 <211> 16 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2447 Ser Val Phe Leu Ile Lys Gly Asp Lys Val Trp Val Tyr Pro Pro Glu 1 5 10 15 <210> 2448 <211> 16 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2448 Val Tyr Pro Pro Glu Lys Lys Glu Lys Gly Tyr Pro Lys Leu Leu Gln 1 5 10 15 <210> 2449 <211> 20 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2449 His Val Gln Pro Gln Pro Gln Pro Lys Pro Gln Val Gln Leu His Val 1 5 10 15 Gln Ser Gln Thr 20 <210> 2450 <211> 32 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2450 Leu Ala Asn Thr Gln Pro Arg Gly Pro Pro Ala Ser Ser Pro Ala Pro 1 5 10 15 Ala Pro Lys Phe Ser Pro Val Thr Pro Lys Phe Thr Pro Val Ala Ser 20 25 30 <210> 2451 <211> 17 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2451 His Val Gln Pro Gln Pro Gln Pro Lys Pro Gln Val Gln Leu His Val 1 5 10 15 Gln <210> 2452 <211> 18 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2452 Ala Ala Pro Arg Pro Ser Pro Ala Ile Ser Val Ser Val Ser Ala Pro 1 5 10 15 Ala Phe <210> 2453 <211> 24 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2453 His Val Gln Pro Gln Pro Gln Pro Lys Pro Gln Val Gln Leu His Val 1 5 10 15 Gln Ser Gln Thr Gln Pro Val Ser 20 <210> 2454 <211> 21 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2454 Val Asn Pro Phe Arg Pro Gly Asp Ser Glu Pro Pro Pro Ala Pro Gly 1 5 10 15 Ala Gln Arg Ala Gln 20 <210> 2455 <211> 25 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2455 Ser Glu Ala Glu Asp Ala Ser Leu Leu Ser Phe Met Gln Gly Tyr Met 1 5 10 15 Lys His Ala Thr Lys Thr Ala Lys Asp 20 25 <210> 2456 <211> 23 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2456 Ser Glu Ala Glu Asp Ala Ser Leu Leu Ser Phe Met Gln Gly Tyr Met 1 5 10 15 Lys His Ala Thr Lys Thr Ala 20 <210> 2457 <211> 39 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2457 Ser Glu Ala Glu Asp Ala Ser Leu Leu Ser Phe Met Gln Gly Tyr Met 1 5 10 15 Lys His Ala Thr Lys Thr Ala Lys Asp Ala Leu Ser Ser Val Gln Glu 20 25 30 Ser Gln Val Ala Gln Gln Ala 35 <210> 2458 <211> 40 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2458 Val Gly Pro Pro Lys Asn Asp Asp Thr Pro Asn Arg Gln Tyr Trp Asp 1 5 10 15 Glu Asp Leu Leu Met Lys Val Leu Glu Tyr Leu Asn Gln Glu Lys Ala 20 25 30 Glu Lys Gly Arg Glu His Ile Ala 35 40 <210> 2459 <211> 42 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2459 Phe Pro Val Gly Pro Pro Lys Asn Asp Asp Thr Pro Asn Arg Gln Tyr 1 5 10 15 Trp Asp Glu Asp Leu Leu Met Lys Val Leu Glu Tyr Leu Asn Gln Glu 20 25 30 Lys Ala Glu Lys Gly Arg Glu His Ile Ala 35 40 <210> 2460 <211> 38 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2460 Val Gly Pro Pro Lys Asn Asp Asp Thr Pro Asn Arg Gln Tyr Trp Asp 1 5 10 15 Glu Asp Leu Leu Met Lys Val Leu Glu Tyr Leu Asn Gln Glu Lys Ala 20 25 30 Glu Lys Gly Arg Glu His 35 <210> 2461 <211> 38 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2461 Gly Gln Gly Ser Ser Glu Asp Asp Leu Gln Glu Glu Glu Gln Ile Glu 1 5 10 15 Gln Ala Ile Lys Glu His Leu Asn Gln Gly Ser Ser Gln Glu Thr Asp 20 25 30 Lys Leu Ala Pro Val Ser 35 <210> 2462 <211> 40 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2462 Val Pro Gly Gln Gly Ser Ser Glu Asp Asp Leu Gln Glu Glu Glu Gln 1 5 10 15 Ile Glu Gln Ala Ile Lys Glu His Leu Asn Gln Gly Ser Ser Gln Glu 20 25 30 Thr Asp Lys Leu Ala Pro Val Ser 35 40 <210> 2463 <211> 13 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2463 Gly Arg Ala Gly Thr Glu Ala Leu Pro Asp Gly Leu Ser 1 5 10 <210> 2464 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2464 Lys His Met Gln Phe Pro Pro Met Tyr Glu 1 5 10 <210> 2465 <211> 23 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2465 Gln Thr Asp Met Ser Arg Lys Ala Phe Val Phe Pro Lys Glu Ser Asp 1 5 10 15 Thr Ser Tyr Val Ser Leu Lys 20 <210> 2466 <211> 27 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2466 Gln Thr Asp Met Ser Arg Lys Ala Phe Val Phe Pro Lys Glu Ser Asp 1 5 10 15 Thr Ser Tyr Val Ser Leu Lys Ala Pro Leu Thr 20 25 <210> 2467 <211> 21 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2467 Gln Thr Asp Met Ser Arg Lys Ala Phe Val Phe Pro Lys Glu Ser Asp 1 5 10 15 Thr Ser Tyr Val Ser 20 <210> 2468 <211> 32 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2468 Asp Ala His Lys Ser Glu Val Ala His Arg Phe Lys Asp Leu Gly Glu 1 5 10 15 Glu Asn Phe Lys Ala Leu Val Leu Ile Ala Phe Ala Gln Tyr Leu Gln 20 25 30 <210> 2469 <211> 20 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2469 Asp Ala His Lys Ser Glu Val Ala His Arg Phe Lys Asp Leu Gly Glu 1 5 10 15 Glu Asn Phe Lys 20 <210> 2470 <211> 24 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2470 Asp Ala His Lys Ser Glu Val Ala His Arg Phe Lys Asp Leu Gly Glu 1 5 10 15 Glu Asn Phe Lys Ala Leu Val Leu 20 <210> 2471 <211> 20 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2471 His Lys Glu Asp Thr Leu Ala Phe Ser Glu Trp Gly Ser Pro His Ala 1 5 10 15 Ala Val Pro Arg 20 <210> 2472 <211> 25 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2472 Leu Glu Pro Val Tyr Pro Gly Asp Asn Ala Thr Pro Glu Gln Met Ala 1 5 10 15 Gln Tyr Ala Ala Asp Leu Arg Arg Tyr 20 25 <210> 2473 <211> 39 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2473 Ala Gln Gly Ala Pro Leu Glu Pro Val Tyr Pro Gly Asp Asn Ala Thr 1 5 10 15 Pro Glu Gln Met Ala Gln Tyr Ala Ala Asp Leu Arg Arg Tyr Ile Asn 20 25 30 Met Leu Thr Arg Pro Arg Tyr 35 <210> 2474 <211> 34 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2474 Leu Glu Pro Val Tyr Pro Gly Asp Asn Ala Thr Pro Glu Gln Met Ala 1 5 10 15 Gln Tyr Ala Ala Asp Leu Arg Arg Tyr Ile Asn Met Leu Thr Arg Pro 20 25 30 Arg Tyr <210> 2475 <211> 37 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2475 Gly Arg Pro Glu Ala Gln Pro Pro Pro Leu Ser Ser Glu His Lys Glu 1 5 10 15 Pro Val Ala Gly Asp Ala Val Pro Gly Pro Lys Asp Gly Ser Ala Pro 20 25 30 Glu Val Arg Gly Ala 35 <210> 2476 <211> 34 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2476 Gly Arg Pro Glu Ala Gln Pro Pro Pro Leu Ser Ser Glu His Lys Glu 1 5 10 15 Pro Val Ala Gly Asp Ala Val Pro Gly Pro Lys Asp Gly Ser Ala Pro 20 25 30 Glu Val <210> 2477 <211> 40 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2477 Ala Pro Pro Gly Arg Pro Glu Ala Gln Pro Pro Pro Leu Ser Ser Glu 1 5 10 15 His Lys Glu Pro Val Ala Gly Asp Ala Val Pro Gly Pro Lys Asp Gly 20 25 30 Ser Ala Pro Glu Val Arg Gly Ala 35 40 <210> 2478 <211> 18 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2478 Ala Pro Pro Glu Pro Val Pro Pro Pro Arg Ala Ala Pro Ala Pro Thr 1 5 10 15 His Val <210> 2479 <211> 19 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2479 Asn Ala Pro Pro Glu Pro Val Pro Pro Pro Arg Ala Ala Pro Ala Pro 1 5 10 15 Thr His Val <210> 2480 <211> 37 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2480 Ala Pro Pro Gly Arg Pro Glu Ala Gln Pro Pro Pro Leu Ser Ser Glu 1 5 10 15 His Lys Glu Pro Val Ala Gly Asp Ala Val Pro Gly Pro Lys Asp Gly 20 25 30 Ser Ala Pro Glu Val 35 <210> 2481 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2481 Ala Glu Ala Leu Leu Thr Glu Thr 1 5 <210> 2482 <211> 38 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2482 Asn Ala Pro Pro Glu Pro Val Pro Pro Pro Arg Ala Ala Pro Ala Pro 1 5 10 15 Thr His Val Arg Ser Pro Gln Pro Pro Pro Pro Ala Pro Ala Pro Ala 20 25 30 Arg Asp Glu Leu Pro Asp 35 <210> 2483 <211> 23 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2483 His Val Thr Asp His Ile His Ala Gly Met Glu Thr Thr Tyr Thr Val 1 5 10 15 Leu Gln Asn Glu Asp Thr Lys 20 <210> 2484 <211> 17 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2484 Lys Glu Lys His Tyr Tyr Ile Gly Ile Ile Glu Thr Thr Trp Asp Tyr 1 5 10 15 Ala <210> 2485 <211> 15 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2485 Ser Pro Ala Ser Ser Thr Thr Ala Arg Val Ile Thr Asn Gln Tyr 1 5 10 15 <210> 2486 <211> 25 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2486 Glu Ile Leu Glu Ser Glu Glu Lys Gly Asp Pro Asn Lys Pro Ser Gly 1 5 10 15 Phe Arg Ser Val Lys Ala Pro Val Thr 20 25 <210> 2487 <211> 29 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2487 Asn Asn Pro Ala Gly Leu Tyr Ser Ser Glu Asn Ile Ser Asn Phe Asn 1 5 10 15 Asn Ala Leu Glu Ser Lys Thr Ala Ala Ser Gly Val Glu 20 25 <210> 2488 <211> 15 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2488 Thr Tyr Ala Pro Val Ile Ser Ala Glu Lys Ala Tyr His Glu Gln 1 5 10 15 <210> 2489 <211> 16 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2489 Thr Tyr Ala Pro Val Ile Ser Ala Glu Lys Ala Tyr His Glu Gln Leu 1 5 10 15 <210> 2490 <211> 16 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2490 Ala Glu Lys Ala Tyr His Glu Gln Leu Ser Val Ala Glu Ile Thr Asn 1 5 10 15 <210> 2491 <211> 31 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2491 Val His Leu Thr Pro Glu Glu Lys Ser Ala Val Thr Ala Leu Trp Gly 1 5 10 15 Lys Val Asn Val Asp Glu Val Gly Gly Glu Ala Leu Gly Arg Leu 20 25 30 <210> 2492 <211> 41 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2492 Val His Leu Thr Pro Glu Glu Lys Ser Ala Val Thr Ala Leu Trp Gly 1 5 10 15 Lys Val Asn Val Asp Glu Val Gly Gly Glu Ala Leu Gly Arg Leu Leu 20 25 30 Val Val Tyr Pro Trp Thr Gln Arg Phe 35 40 <210> 2493 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2493 Leu Val Val Tyr Pro Trp Thr Gln Arg Phe 1 5 10 <210> 2494 <211> 22 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2494 Val Gly Gly Thr Gly Gly Ile Gly Gly Val Gly Gly Thr Gly Gly Val 1 5 10 15 Gly Asn Arg Ala Pro Arg 20 <210> 2495 <211> 21 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2495 Gly Gly Thr Gly Gly Ile Gly Gly Val Gly Gly Thr Gly Gly Val Gly 1 5 10 15 Asn Arg Ala Pro Arg 20 <210> 2496 <211> 21 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2496 Val Gly Gly Thr Gly Gly Ile Gly Gly Val Gly Gly Thr Gly Gly Val 1 5 10 15 Gly Asn Arg Ala Pro 20 <210> 2497 <211> 23 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2497 Thr Val Gly Gly Thr Gly Gly Ile Gly Gly Val Gly Gly Thr Gly Gly 1 5 10 15 Val Gly Asn Arg Ala Pro Arg 20 <210> 2498 <211> 35 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2498 Phe Glu Ile Pro Ile Asn Gly Leu Ser Glu Phe Val Asp Tyr Glu Asp 1 5 10 15 Leu Val Glu Leu Ala Pro Gly Lys Phe Gln Leu Val Ala Glu Asn Arg 20 25 30 Arg Tyr Gln 35 <210> 2499 <211> 31 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2499 Ser Ile Leu Gln Met Ser Leu Asp His His Ile Val Thr Pro Leu Thr 1 5 10 15 Ser Leu Val Ile Glu Asn Glu Ala Gly Asp Glu Arg Met Leu Ala 20 25 30 <210> 2500 <211> 34 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2500 Ala Ser His Thr Ser Asp Ser Asp Val Pro Ser Gly Val Thr Glu Val 1 5 10 15 Val Val Lys Leu Phe Asp Ser Asp Pro Ile Thr Val Thr Val Pro Val 20 25 30 Glu Val <210> 2501 <211> 23 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2501 Ala Ile Gln Leu Thr Tyr Asn Pro Asp Glu Ser Ser Lys Pro Asn Met 1 5 10 15 Ile Asp Ala Ala Thr Leu Lys 20 <210> 2502 <211> 21 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2502 His Leu Ser Pro Thr Gly Thr Thr Glu Phe Trp Leu Gly Asn Glu Lys 1 5 10 15 Ile His Leu Ile Ser 20 <210> 2503 <211> 11 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2503 Ser Tyr Val Leu Thr Gln Pro Pro Ser Val Ser 1 5 10 <210> 2504 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2504 Tyr Val Leu Thr Gln Pro Pro Ser Val Ser 1 5 10 <210> 2505 <211> 23 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2505 Ser Glu Thr Ala Pro Ala Ala Pro Ala Ala Pro Ala Pro Ala Glu Lys 1 5 10 15 Thr Pro Val Lys Lys Lys Ala 20 <210> 2506 <211> 19 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2506 Ser Glu Thr Ala Pro Ala Ala Pro Ala Ala Pro Ala Pro Ala Glu Lys 1 5 10 15 Thr Pro Val <210> 2507 <211> 20 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2507 Ser Glu Thr Ala Pro Ala Ala Pro Ala Ala Pro Ala Pro Ala Glu Lys 1 5 10 15 Thr Pro Val Lys 20 <210> 2508 <211> 14 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2508 Thr His Phe Gly Val Leu Met Asp Leu Pro Arg Ser Ala Ser 1 5 10 <210> 2509 <211> 18 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2509 Thr His Phe Gly Val Leu Met Asp Leu Pro Arg Ser Ala Ser Gln Leu 1 5 10 15 Asp Ala <210> 2510 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2510 Tyr Glu Leu Thr Gln Pro Pro Ser Val Ser 1 5 10 <210> 2511 <211> 11 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2511 Ser Tyr Glu Leu Thr Gln Pro Pro Ser Val Ser 1 5 10 <210> 2512 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2512 Ser Val Leu Thr Gln Pro Pro Ser Val Ser 1 5 10 <210> 2513 <211> 7 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2513 Thr Gln Pro Pro Ser Val Ser 1 5 <210> 2514 <211> 11 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2514 Gln Ser Val Leu Thr Gln Pro Pro Ser Val Ser 1 5 10 <210> 2515 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2515 Ser Val Leu Thr Gln Pro Pro Ser Val Ser 1 5 10 <210> 2516 <211> 7 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2516 Thr Gln Pro Pro Ser Val Ser 1 5 <210> 2517 <211> 16 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2517 Thr Pro Leu Gly Pro Lys Trp Pro Glu Pro Val Phe Gly Arg Leu Ala 1 5 10 15 <210> 2518 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2518 Glu Ile Val Leu Thr Gln Ser Pro Gly Thr Leu Ser 1 5 10 <210> 2519 <211> 11 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2519 Ile Val Leu Thr Gln Ser Pro Gly Thr Leu Ser 1 5 10 <210> 2520 <211> 14 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2520 Asp Val Val Met Thr Gln Ser Pro Leu Ser Leu Pro Val Thr 1 5 10 <210> 2521 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2521 Asp Val Val Met Thr Gln Ser Pro Leu Ser 1 5 10 <210> 2522 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2522 Phe Phe Gln Tyr Asp Thr Trp Lys Gln Ser Thr Gln 1 5 10 <210> 2523 <211> 14 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2523 Phe Phe Gln Tyr Asp Thr Trp Lys Gln Ser Thr Gln Arg Leu 1 5 10 <210> 2524 <211> 11 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2524 Ser Tyr Phe Val Glu Leu Gly Thr Gln Pro Ala 1 5 10 <210> 2525 <211> 19 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2525 Gly Thr Glu Leu Val Asn Phe Leu Ser Tyr Phe Val Glu Leu Gly Thr 1 5 10 15 Gln Pro Ala <210> 2526 <211> 16 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2526 Thr Asp Tyr Gly Lys Asp Leu Met Glu Lys Val Lys Ser Pro Glu Leu 1 5 10 15 <210> 2527 <211> 14 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2527 Asp Ile Val Met Thr Gln Thr Pro Leu Ser Ser Pro Val Thr 1 5 10 <210> 2528 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2528 Asp Ile Val Met Thr Gln Thr Pro Leu Ser 1 5 10 <210> 2529 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2529 Ser Glu Tyr Gln Thr Phe Phe Asn Pro Arg 1 5 10 <210> 2530 <211> 9 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2530 Glu Tyr Gln Thr Phe Phe Asn Pro Arg 1 5 <210> 2531 <211> 17 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2531 Gln His Val Phe Leu Ala Pro Gln Gln Ala Arg Ser Leu Leu Gln Arg 1 5 10 15 Val <210> 2532 <211> 17 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2532 Thr Val Phe Leu Asp His Glu Asn Ala Asn Lys Ile Leu Asn Arg Pro 1 5 10 15 Lys <210> 2533 <211> 15 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2533 Phe Leu Asp His Glu Asn Ala Asn Lys Ile Leu Asn Arg Pro Lys 1 5 10 15 <210> 2534 <211> 26 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2534 Glu Glu Ala Gly Ala Arg Val Gln Gln Asn Val Pro Ser Gly Thr Asp 1 5 10 15 Thr Gly Asp Pro Gln Ser Lys Pro Leu Gly 20 25 <210> 2535 <211> 24 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2535 Glu Glu Ala Gly Ala Arg Val Gln Gln Asn Val Pro Ser Gly Thr Asp 1 5 10 15 Thr Gly Asp Pro Gln Ser Lys Pro 20 <210> 2536 <211> 21 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2536 Ile Glu Thr Lys Gly Gln Tyr Asp Glu Glu Glu Met Thr Met Gln Gln 1 5 10 15 Ala Lys Arg Arg Gln 20 <210> 2537 <211> 24 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2537 Glu Leu Arg Ile Glu Thr Lys Gly Gln Tyr Asp Glu Glu Glu Glu Met Thr 1 5 10 15 Met Gln Gln Ala Lys Arg Arg Gln 20 <210> 2538 <211> 27 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2538 Ala Gln Pro Gln Phe Val His Pro Glu His Arg Ser Phe Val Asp Leu 1 5 10 15 Ser Gly His Asn Leu Ala Asn Pro His Pro Phe 20 25 <210> 2539 <211> 29 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2539 Met Ala Ala Gln Pro Gln Phe Val His Pro Glu His Arg Ser Phe Val 1 5 10 15 Asp Leu Ser Gly His Asn Leu Ala Asn Pro His Pro Phe 20 25 <210> 2540 <211> 15 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2540 Val Ala Trp Lys Ala Asp Ser Ser Pro Val Lys Ala Gly Val Glu 1 5 10 15 <210> 2541 <211> 34 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2541 Val Ala Trp Lys Ala Asp Ser Ser Pro Val Lys Ala Gly Val Glu Thr 1 5 10 15 Thr Thr Pro Ser Lys Gln Ser Asn Asn Lys Tyr Ala Ala Ser Ser Tyr 20 25 30 Leu Ser <210> 2542 <211> 23 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2542 Ala Gly Val Glu Thr Thr Thr Thr Pro Ser Lys Gln Ser Asn Asn Lys Tyr 1 5 10 15 Ala Ala Ser Ser Tyr Leu Ser 20 <210> 2543 <211> 16 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2543 Gln Glu Gln Thr Tyr Val Ile Ser Ala Pro Lys Ile Phe Arg Val Gly 1 5 10 15 <210> 2544 <211> 19 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2544 Leu Ser Phe Ser Pro Ser Gln Ser Leu Pro Ala Ser His Ala His Leu 1 5 10 15 Arg Val Thr <210> 2545 <211> 17 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2545 Ser Val Ser Gly Lys Pro Gln Tyr Met Val Leu Val Pro Ser Leu Leu 1 5 10 15 His <210> 2546 <211> 15 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2546 Ala Gln Gln Ala Ala Asp Lys Tyr Leu Tyr Val Asp Lys Asn Phe 1 5 10 15 <210> 2547 <211> 30 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2547 Thr Gly Leu Ser Met Asp Gly Gly Gly Ser Pro Lys Gly Asp Val Asp 1 5 10 15 Pro Phe Tyr Tyr Asp Tyr Glu Thr Val Arg Asn Gly Gly Leu 20 25 30 <210> 2548 <211> 17 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2548 Thr Gly Leu Ser Met Asp Gly Gly Gly Ser Pro Lys Gly Asp Val Asp 1 5 10 15 Pro <210> 2549 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2549 Asp Ile Val Met Thr Gln Ser Pro Leu Ser 1 5 10 <210> 2550 <211> 14 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2550 Asp Ile Val Met Thr Gln Ser Pro Leu Ser Leu Pro Val Thr 1 5 10 <210> 2551 <211> 37 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2551 Ser Glu Thr Ser Arg Thr Ala Phe Gly Gly Arg Arg Ala Val Pro Pro 1 5 10 15 Asn Asn Ser Asn Ala Ala Glu Asp Asp Leu Pro Thr Val Glu Leu Gln 20 25 30 Gly Val Val Pro Arg 35 <210> 2552 <211> 31 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2552 Glu Ala Glu Asp Leu Gln Val Gly Gln Val Glu Leu Gly Gly Gly Pro 1 5 10 15 Gly Ala Gly Ser Leu Gln Pro Leu Ala Leu Glu Gly Ser Leu Gln 20 25 30 <210> 2553 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2553 Glu Ile Val Leu Thr Gln Ser Pro Ala Thr Leu Ser 1 5 10 <210> 2554 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2554 Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser 1 5 10 <210> 2555 <211> 9 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2555 Phe Ser Phe Leu Pro Gln Pro Pro Gln 1 5 <210> 2556 <211> 20 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2556 Gln Glu Glu Ala Gln Ser Trp Gly His Ser Ser Glu Gln Asp Gly Leu 1 5 10 15 Arg Val Pro Arg 20 <210> 2557 <211> 33 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2557 Gln Arg Asp Pro Val Gly Arg Tyr Glu Pro Ala Gly Gly Asp Ala Asn 1 5 10 15 Arg Leu Arg Arg Pro Gly Gly Ser Tyr Pro Ala Ala Ala Ala Ala Lys 20 25 30 Val <210> 2558 <211> 23 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2558 Gln Arg Asp Pro Val Gly Arg Tyr Glu Pro Ala Gly Gly Asp Ala Asn 1 5 10 15 Arg Leu Arg Arg Pro Gly Gly 20 <210> 2559 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2559 Gln Ile Phe Leu Pro Glu Pro Glu Gln Pro Ser Arg 1 5 10 <210> 2560 <211> 24 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2560 Ile Val Arg Gly Asp Gln Pro Ala Ala Ser Gly Asp Ser Asp Asp Asp 1 5 10 15 Glu Pro Pro Pro Leu Pro Arg Leu 20 <210> 2561 <211> 11 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2561 Asn Phe Met Leu Thr Gln Pro His Ser Val Ser 1 5 10 <210> 2562 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2562 Phe Met Leu Thr Gln Pro His Ser Val Ser 1 5 10 <210> 2563 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2563 Glu Ile Val Met Thr Gln Ser Pro Ala Thr Leu Ser 1 5 10 <210> 2564 <211> 13 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2564 Ser Val Leu Leu Ala Gln Glu Leu Pro Gln Gln Leu Thr 1 5 10 <210> 2565 <211> 24 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2565 Ser Glu Thr Ala Pro Ala Ala Pro Ala Ala Ala Pro Pro Ala Glu Lys 1 5 10 15 Ala Pro Val Lys Lys Lys Ala Ala 20 <210> 2566 <211> 23 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2566 Thr Glu Lys Ala Pro Glu Pro His Val Glu Glu Asp Asp Asp Asp Glu 1 5 10 15 Leu Asp Ser Lys Leu Asn Tyr 20 <210> 2567 <211> 43 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2567 Glu Ala Pro Tyr Gly Ala Pro Arg Phe Asp Met Pro Asp Phe Glu Asp 1 5 10 15 Asp Gly Gly Pro Tyr Gly Glu Ser Glu Ala Pro Ala Pro Pro Gly Pro 20 25 30 Gly Thr Arg Trp Pro Tyr Arg Ser Arg Asp Thr 35 40 <210> 2568 <211> 24 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2568 Asp Asp Ile Leu Ala Ser Pro Pro Arg Leu Pro Glu Pro Gln Pro Tyr 1 5 10 15 Pro Gly Ala Pro His His Ser Ser 20 <210> 2569 <211> 11 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2569 Gln Ser Ala Leu Thr Gln Pro Pro Ser Val Ser 1 5 10 <210> 2570 <211> 7 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2570 Thr Gln Pro Pro Ser Val Ser 1 5 <210> 2571 <211> 33 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2571 Gln Gln Tyr Asn Arg Val Gly Lys Val Glu His Gly Ser Val Ala Leu 1 5 10 15 Pro Ala Ile Met Arg Ser Gly Ala Ser Gly Pro Glu Asn Phe Gln Val 20 25 30 Gly <210> 2572 <211> 43 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2572 Ala Asp Ala Ser Glu Ala His Glu Ser Ser Ser Arg Gly Glu Ala Gly 1 5 10 15 Ala Pro Gly Glu Glu Asp Ile Gln Gly Pro Thr Lys Ala Asp Thr Glu 20 25 30 Lys Trp Ala Glu Gly Gly Gly His Ser Arg Glu 35 40 <210> 2573 <211> 17 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2573 Glu Pro Leu Gln Ala Arg Ala Asp Glu Val Ala Ala Ala Pro Glu Gln 1 5 10 15 Ile <210> 2574 <211> 9 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2574 Gln Glu Phe Pro Asp Pro Glu Lys Phe 1 5 <210> 2575 <211> 30 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2575 Glu Lys Lys Glu Gly His Phe Ser Ala Leu Pro Ser Leu Pro Val Gly 1 5 10 15 Ser His Ala Lys Val Ser Ser Pro Gln Pro Arg Gly Pro Arg 20 25 30 <210> 2576 <211> 19 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2576 Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Lys Pro Gly Gly 1 5 10 15 Ser Leu Arg <210> 2577 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2577 Ser Ala Leu Thr Gln Pro Arg Ser Val Ser 1 5 10 <210> 2578 <211> 9 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2578 Lys Leu Met Pro Pro Pro Pro Pro Pro 1 5 <210> 2579 <211> 18 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2579 Asp Gly Pro Pro Gly Leu Pro Gly Thr Pro Gly Pro Pro Gly Pro Pro 1 5 10 15 Gly Pro <210> 2580 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2580 Arg Pro Pro Gly Phe Ser Pro Phe 1 5 <210> 2581 <211> 9 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2581 Phe Glu Asn Lys Phe Ala Val Glu Thr 1 5 <210> 2582 <211> 33 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2582 Arg His Lys Ala Gln Pro Ala His Glu Ala Val Glu Lys Glu Thr Thr 1 5 10 15 Glu Lys Glu Ala Thr Glu Lys Glu Ala Glu Ile Val Glu Ala Asp Lys 20 25 30 Glu <210> 2583 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2583 Tyr Glu Leu Thr Gln Pro Ser Ser Val Ser 1 5 10 <210> 2584 <211> 6 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2584 Gln Pro Leu Ser Phe Gln 1 5 <210> 2585 <211> 22 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2585 Thr Ile Val Glu Glu Val Gln Asp Gly Lys Val Ile Ser Ser Arg Glu 1 5 10 15 Gln Val His Gln Thr Thr 20 <210> 2586 <211> 17 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2586 Ser Val Val Pro Ser Pro Lys Val Ser Asp Thr Val Val Glu Pro Tyr 1 5 10 15 Asn <210> 2587 <211> 29 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2587 Ala Ala Pro Gly Gln Glu Pro Pro Glu His Met Ala Glu Leu Gln Arg 1 5 10 15 Asn Glu Gln Glu Gln Pro Leu Gly Gln Trp His Leu Ser 20 25 <210> 2588 <211> 13 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2588 Asp Ile Val Met Thr Gln Ser Pro Asp Ser Leu Ala Val 1 5 10 <210> 2589 <211> 13 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2589 Ser Ile Pro Ile Pro Gln Lys Leu Phe Gly Glu Val Thr 1 5 10 <210> 2590 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2590 Gln Ser Ala Thr Ser Pro Ser Pro 1 5 <210> 2591 <211> 6 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2591 Thr Val Ser Pro Pro Gly 1 5 <210> 2592 <211> 14 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2592 Ser Lys Gln Pro Pro Pro Gln Pro Gln His Thr Pro Ser Pro 1 5 10 <210> 2593 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2593 Glu Gly Asp Phe Leu Ala Glu Gly Gly Gly Val Arg 1 5 10 <210> 2594 <211> 15 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2594 Asp Ser Gly Glu Gly Asp Phe Leu Ala Glu Gly Gly Gly Val Arg 1 5 10 15 <210> 2595 <211> 16 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2595 Asn Gly Phe Lys Ser His Ala Leu Gln Leu Asn Asn Arg Gln Ile Arg 1 5 10 15 <210> 2596 <211> 17 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2596 Ser Ser Lys Ile Thr His Arg Ile His Trp Glu Ser Ala Ser Leu Leu 1 5 10 15 Arg <210> 2597 <211> 31 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2597 Ser Tyr Lys Met Ala Asp Glu Ala Gly Ser Glu Ala Asp His Glu Gly 1 5 10 15 Thr His Ser Thr Lys Arg Gly His Ala Lys Ser Arg Pro Val Arg 20 25 30 <210> 2598 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2598 Lys Asn Gly Glu Thr Gly Pro Gln Gly Pro 1 5 10 <210> 2599 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2599 Lys Thr Phe Gly Lys Met Lys Pro Arg Tyr 1 5 10 <210> 2600 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2600 Val Lys Gly Asp Arg Gly Glu Thr Gly Ala 1 5 10 <210> 2601 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2601 Arg Ser Ser Arg Ile Gly Glu Ile Lys Glu 1 5 10 <210> 2602 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2602 Gln Ile Arg Gly Leu Glu Glu Glu Leu Gln 1 5 10 <210> 2603 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2603 Ser Ser Arg Ile Gly Glu Ile Lys Glu Glu 1 5 10 <210> 2604 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2604 Ser Glu Glu Thr Lys Glu Asn Glu Gly Phe 1 5 10 <210> 2605 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2605 Ser Leu Leu Arg Ser Glu Glu Thr Lys Glu 1 5 10 <210> 2606 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2606 Gly Leu Glu Glu Glu Leu Gln Phe Ser Leu 1 5 10 <210> 2607 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2607 Ser Glu Glu Thr Lys Glu Asn Glu Gly Phe 1 5 10 <210> 2608 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2608 Gly Leu Glu Glu Glu Leu Gln Phe Ser Leu 1 5 10 <210> 2609 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2609 Ser Leu Leu Arg Ser Glu Glu Thr Lys Glu 1 5 10 <210> 2610 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2610 Asn Gln Glu Gln Val Ser Pro Leu Thr Leu 1 5 10 <210> 2611 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2611 Lys His Asn Leu Gly His Gly His Lys His 1 5 10 <210> 2612 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2612 Ser Glu Glu Thr Lys Glu Asn Glu Gly Phe 1 5 10 <210> 2613 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2613 Ser Leu Leu Arg Ser Glu Glu Thr Lys Glu 1 5 10 <210> 2614 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2614 Ile Asn Val Lys Val Gly Gly Asn Ser Lys 1 5 10 <210> 2615 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2615 Gly Leu Glu Glu Glu Leu Gln Phe Ser Leu 1 5 10 <210> 2616 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2616 Ser Leu Leu Arg Ser Glu Glu Thr Lys Glu 1 5 10 <210> 2617 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2617 Gln Ile Arg Gly Leu Glu Glu Glu Leu Gln 1 5 10 <210> 2618 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2618 Arg Ser Leu Met Pro Phe Ser Pro Tyr Glu 1 5 10 <210> 2619 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2619 Tyr Trp Glu Val Gln Pro Ala Thr Phe Arg 1 5 10 <210> 2620 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2620 Thr Gly Lys Leu Pro Tyr Gly Tyr Gly Pro 1 5 10 <210> 2621 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2621 Gly Leu Ser Pro Ile Phe Pro Gly Gly Ala 1 5 10 <210> 2622 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2622 Tyr Lys Met Ala Asp Glu Ala Gly Ser Glu 1 5 10 <210> 2623 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2623 Lys Met Ala Asp Glu Ala Gly Ser Glu Ala 1 5 10 <210> 2624 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2624 Lys Ser Ser Ser Tyr Ser Lys Gln Phe Thr 1 5 10 <210> 2625 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2625 Ala Asp Glu Ala Gly Ser Glu Ala Asp His 1 5 10 <210> 2626 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2626 Gly Pro Arg Val Val Glu Arg His Gln Ser 1 5 10 <210> 2627 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2627 Gly Pro Arg Val Val Glu Arg His Gln Ser 1 5 10 <210> 2628 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2628 Arg Gly Pro Arg Val Val Glu Arg His Gln 1 5 10 <210> 2629 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2629 Asp Asn Thr Tyr Asn Arg Val Ser Glu Asp 1 5 10 <210> 2630 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2630 Gly Pro Arg Val Val Glu Arg His Gln Ser 1 5 10 <210> 2631 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2631 Asp Glu Ala Gly Ser Glu Ala Asp His Glu 1 5 10 <210> 2632 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2632 Arg Gly Pro Arg Val Val Glu Arg His Gln 1 5 10 <210> 2633 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2633 Leu Glu Arg Pro Gly Gly Asn Glu Ile Thr 1 5 10 <210> 2634 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2634 Gly Pro Arg Val Val Glu Arg His Gln Ser 1 5 10 <210> 2635 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2635 Gly Ser Thr Gly Ser Trp Asn Ser Gly Ser 1 5 10 <210> 2636 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2636 Gly Pro Arg Val Val Glu Arg His Gln Ser 1 5 10 <210> 2637 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2637 Asp Glu Ala Gly Ser Glu Ala Asp His Glu 1 5 10 <210> 2638 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2638 Lys Ser Tyr Lys Met Ala Asp Glu Ala Gly 1 5 10 <210> 2639 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2639 Glu Arg His Gln Ser Ala Cys Lys Asp Ser 1 5 10 <210> 2640 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2640 Ala Leu Thr Asp Met Pro Gln Met Arg Met 1 5 10 <210> 2641 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2641 Ser Gln Leu Gln Lys Val Pro Pro Glu Trp 1 5 10 <210> 2642 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2642 Gly Pro Arg Val Val Glu Arg His Gln Ser 1 5 10 <210> 2643 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2643 Val Glu Arg His Gln Ser Ala Cys Lys Asp 1 5 10 <210> 2644 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2644 Lys Ser Ser Ser Tyr Ser Lys Gln Phe Thr 1 5 10 <210> 2645 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2645 Ser Gln Leu Gln Lys Val Pro Pro Glu Trp 1 5 10 <210> 2646 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2646 Lys Val Pro Pro Glu Trp Lys Ala Leu Thr 1 5 10 <210> 2647 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2647 Gly Ser Thr Gly Ser Trp Asn Ser Gly Ser 1 5 10 <210> 2648 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2648 Leu Glu Arg Pro Gly Gly Asn Glu Ile Thr 1 5 10 <210> 2649 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2649 Lys Ser Ser Ser Tyr Ser Lys Gln Phe Thr 1 5 10 <210> 2650 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2650 Glu Arg His Gln Ser Ala Cys Lys Asp Ser 1 5 10 <210> 2651 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2651 Arg Asp Asn Thr Tyr Asn Arg Val Ser Glu 1 5 10 <210> 2652 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2652 Arg His Gln Ser Ala Cys Lys Asp Ser Asp 1 5 10 <210> 2653 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2653 Asp Met Pro Gln Met Arg Met Glu Leu Glu 1 5 10 <210> 2654 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2654 Glu Glu Val Ser Gly Asn Val Ser Pro Gly 1 5 10 <210> 2655 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2655 Lys Ser Gln Leu Gln Lys Val Pro Pro Glu 1 5 10 <210> 2656 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2656 Pro Ser Ser Ala Gly Ser Trp Asn Ser Gly 1 5 10 <210> 2657 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2657 Lys Ser Gln Leu Gln Lys Val Pro Pro Glu 1 5 10 <210> 2658 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2658 Met Glu Leu Glu Arg Pro Gly Gly Asn Glu 1 5 10 <210> 2659 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2659 Ser Ala Cys Lys Asp Ser Asp Trp Pro Phe 1 5 10 <210> 2660 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2660 Asp Met Pro Gln Met Arg Met Glu Leu Glu 1 5 10 <210> 2661 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2661 Lys Ser Tyr Lys Met Ala Asp Glu Ala Gly 1 5 10 <210> 2662 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2662 Lys Ser Ser Ser Tyr Ser Lys Gln Phe Thr 1 5 10 <210> 2663 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2663 Pro Gly Ser Ser Gly Thr Gly Gly Thr Ala 1 5 10 <210> 2664 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2664 Lys Met Ala Asp Glu Ala Gly Ser Glu Ala 1 5 10 <210> 2665 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2665 Glu Glu Val Ser Gly Asn Val Ser Pro Gly 1 5 10 <210> 2666 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2666 Lys Ser Ser Ser Tyr Ser Lys Gln Phe Thr 1 5 10 <210> 2667 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2667 Arg Pro Gly Gly Asn Glu Ile Thr Arg Gly 1 5 10 <210> 2668 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2668 Lys Gly Asp Lys Glu Leu Arg Thr Gly Lys 1 5 10 <210> 2669 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2669 Ser Gly Ser Ser Gly Pro Gly Ser Thr Gly 1 5 10 <210> 2670 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2670 Phe Phe Ser Pro Met Leu Gly Glu Phe Val 1 5 10 <210> 2671 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2671 Lys Ser Arg Pro Val Arg Asp Cys Asp Asp 1 5 10 <210> 2672 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2672 Lys Ser Gln Leu Gln Lys Val Pro Pro Glu 1 5 10 <210> 2673 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2673 Ser Asn Ser Thr Asn Ile Phe Phe Ser Pro 1 5 10 <210> 2674 <211> 21 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2674 Met Ile Glu Gln Asn Thr Lys Ser Pro Leu Phe Met Gly Lys Val Val 1 5 10 15 Asn Pro Thr Gln Lys 20 <210> 2675 <211> 40 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2675 Ala Ile Pro Met Ser Ile Pro Pro Glu Val Lys Phe Asn Lys Pro Phe 1 5 10 15 Val Phe Leu Met Ile Glu Gln Asn Thr Lys Ser Pro Leu Phe Met Gly 20 25 30 Lys Val Val Asn Pro Thr Gln Lys 35 40 <210> 2676 <211> 35 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2676 Ile Pro Pro Glu Val Lys Phe Asn Lys Pro Phe Val Phe Leu Met Ile 1 5 10 15 Glu Gln Asn Thr Lys Ser Pro Leu Phe Met Gly Lys Val Val Asn Pro 20 25 30 Thr Gln Lys 35 <210> 2677 <211> 47 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2677 Ala Gly Ala Met Phe Leu Glu Ala Ile Pro Met Ser Ile Pro Pro Glu 1 5 10 15 Val Lys Phe Asn Lys Pro Phe Val Phe Leu Met Ile Glu Gln Asn Thr 20 25 30 Lys Ser Pro Leu Phe Met Gly Lys Val Val Asn Pro Thr Gln Lys 35 40 45 <210> 2678 <211> 36 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2678 Ser Ile Pro Pro Glu Val Lys Phe Asn Lys Pro Phe Val Phe Leu Met 1 5 10 15 Ile Glu Gln Asn Thr Lys Ser Pro Leu Phe Met Gly Lys Val Val Asn 20 25 30 Pro Thr Gln Lys 35 <210> 2679 <211> 22 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2679 Leu Met Ile Glu Gln Asn Thr Lys Ser Pro Leu Phe Met Gly Lys Val 1 5 10 15 Val Asn Pro Thr Gln Lys 20 <210> 2680 <211> 29 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2680 Phe Asn Lys Pro Phe Val Phe Leu Met Ile Glu Gln Asn Thr Lys Ser 1 5 10 15 Pro Leu Phe Met Gly Lys Val Val Asn Pro Thr Gln Lys 20 25 <210> 2681 <211> 41 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2681 Glu Ala Ile Pro Met Ser Ile Pro Pro Glu Val Lys Phe Asn Lys Pro 1 5 10 15 Phe Val Phe Leu Met Ile Glu Gln Asn Thr Lys Ser Pro Leu Phe Met 20 25 30 Gly Lys Val Val Asn Pro Thr Gln Lys 35 40 <210> 2682 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2682 Ser Asn Ser Thr Asn Ile Phe Phe Ser Pro 1 5 10 <210> 2683 <211> 20 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2683 Ile Glu Gln Asn Thr Lys Ser Pro Leu Phe Met Gly Lys Val Val Asn 1 5 10 15 Pro Thr Gln Lys 20 <210> 2684 <211> 44 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2684 Met Phe Leu Glu Ala Ile Pro Met Ser Ile Pro Pro Glu Val Lys Phe 1 5 10 15 Asn Lys Pro Phe Val Phe Leu Met Ile Glu Gln Asn Thr Lys Ser Pro 20 25 30 Leu Phe Met Gly Lys Val Val Asn Pro Thr Gln Lys 35 40 <210> 2685 <211> 37 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2685 Met Ser Ile Pro Pro Glu Val Lys Phe Asn Lys Pro Phe Val Phe Leu 1 5 10 15 Met Ile Glu Gln Asn Thr Lys Ser Pro Leu Phe Met Gly Lys Val Val 20 25 30 Asn Pro Thr Gln Lys 35 <210> 2686 <211> 43 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2686 Phe Leu Glu Ala Ile Pro Met Ser Ile Pro Pro Glu Val Lys Phe Asn 1 5 10 15 Lys Pro Phe Val Phe Leu Met Ile Glu Gln Asn Thr Lys Ser Pro Leu 20 25 30 Phe Met Gly Lys Val Val Asn Pro Thr Gln Lys 35 40 <210> 2687 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2687 Asn Ser Thr Asn Ile Phe Phe Ser Pro Val 1 5 10 <210> 2688 <211> 50 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2688 Thr Glu Ala Ala Gly Ala Met Phe Leu Glu Ala Ile Pro Met Ser Ile 1 5 10 15 Pro Pro Glu Val Lys Phe Asn Lys Pro Phe Val Phe Leu Met Ile Glu 20 25 30 Gln Asn Thr Lys Ser Pro Leu Phe Met Gly Lys Val Val Asn Pro Thr 35 40 45 Gln Lys 50 <210> 2689 <211> 49 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2689 Glu Ala Ala Gly Ala Met Phe Leu Glu Ala Ile Pro Met Ser Ile Pro 1 5 10 15 Pro Glu Val Lys Phe Asn Lys Pro Phe Val Phe Leu Met Ile Glu Gln 20 25 30 Asn Thr Lys Ser Pro Leu Phe Met Gly Lys Val Val Asn Pro Thr Gln 35 40 45 Lys <210> 2690 <211> 41 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2690 Glu Ala Ile Pro Met Ser Ile Pro Pro Glu Val Lys Phe Asn Lys Pro 1 5 10 15 Phe Val Phe Leu Met Ile Glu Gln Asn Thr Lys Ser Pro Leu Phe Met 20 25 30 Gly Lys Val Val Asn Pro Thr Gln Lys 35 40 <210> 2691 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2691 Asn Ser Thr Asn Ile Phe Phe Ser Pro Val 1 5 10 <210> 2692 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2692 Gln Ser Asn Ser Thr Asn Ile Phe Phe Ser 1 5 10 <210> 2693 <211> 48 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2693 Ala Ala Gly Ala Met Phe Leu Glu Ala Ile Pro Met Ser Ile Pro Pro 1 5 10 15 Glu Val Lys Phe Asn Lys Pro Phe Val Phe Leu Met Ile Glu Gln Asn 20 25 30 Thr Lys Ser Pro Leu Phe Met Gly Lys Val Val Asn Pro Thr Gln Lys 35 40 45 <210> 2694 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2694 Gln Ser Asn Ser Thr Asn Ile Phe Phe Ser 1 5 10 <210> 2695 <211> 46 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2695 Gly Ala Met Phe Leu Glu Ala Ile Pro Met Ser Ile Pro Pro Glu Val 1 5 10 15 Lys Phe Asn Lys Pro Phe Val Phe Leu Met Ile Glu Gln Asn Thr Lys 20 25 30 Ser Pro Leu Phe Met Gly Lys Val Val Asn Pro Thr Gln Lys 35 40 45 <210> 2696 <211> 51 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2696 Gly Thr Glu Ala Ala Gly Ala Met Phe Leu Glu Ala Ile Pro Met Ser 1 5 10 15 Ile Pro Pro Glu Val Lys Phe Asn Lys Pro Phe Val Phe Leu Met Ile 20 25 30 Glu Gln Asn Thr Lys Ser Pro Leu Phe Met Gly Lys Val Val Asn Pro 35 40 45 Thr Gln Lys 50 <210> 2697 <211> 45 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2697 Ala Met Phe Leu Glu Ala Ile Pro Met Ser Ile Pro Pro Glu Val Lys 1 5 10 15 Phe Asn Lys Pro Phe Val Phe Leu Met Ile Glu Gln Asn Thr Lys Ser 20 25 30 Pro Leu Phe Met Gly Lys Val Val Asn Pro Thr Gln Lys 35 40 45 <210> 2698 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2698 His Gln Ser Asn Ser Thr Asn Ile Phe Phe 1 5 10 <210> 2699 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2699 Ser Asn Ser Thr Asn Ile Phe Phe Ser Pro 1 5 10 <210> 2700 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2700 Gly Ser Val Phe Leu Arg Asn Pro Ser Arg 1 5 10 <210> 2701 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2701 Gln Val Val Lys Gly Ser Val Phe Leu Arg 1 5 10 <210> 2702 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2702 Asn Val Pro Cys Ser Pro Lys Val Asp Phe 1 5 10 <210> 2703 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2703 Val Pro Cys Ser Pro Lys Val Asp Phe Thr 1 5 10 <210> 2704 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2704 Val Gly Val Gln Leu Gln Asp Val Pro Arg 1 5 10 <210> 2705 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2705 Leu Arg Asn Pro Ser Arg Asn Asn Val Pro 1 5 10 <210> 2706 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2706 Asp Val Pro Arg Gly Gln Val Val Lys Gly 1 5 10 <210> 2707 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2707 Leu Gln Asp Val Pro Arg Gly Gln Val Val 1 5 10 <210> 2708 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2708 Arg Gly Leu Glu Glu Glu Leu Gln Phe Ser 1 5 10 <210> 2709 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2709 Val Pro Leu Ser Val Gly Val Gln Leu Gln 1 5 10 <210> 2710 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2710 Gly Leu Glu Glu Glu Leu Gln Phe Ser Leu 1 5 10 <210> 2711 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2711 Arg Arg Arg Arg Glu Ala Pro Lys Val Val 1 5 10 <210> 2712 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2712 Leu Gly Val Pro Leu Ser Val Gly Val Gln 1 5 10 <210> 2713 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2713 Val Gly Gly Asn Ser Lys Gly Thr Leu Lys 1 5 10 <210> 2714 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2714 Leu Gln Leu Phe Glu Gly Arg Arg Asn Arg 1 5 10 <210> 2715 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2715 Leu Gln Leu Phe Glu Gly Arg Arg Asn Arg 1 5 10 <210> 2716 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2716 Arg Gly Leu Glu Glu Glu Leu Gln Phe Ser 1 5 10 <210> 2717 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2717 Leu Phe Glu Gly Arg Arg Asn Arg Arg Arg 1 5 10 <210> 2718 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2718 Asn Pro Ser Arg Asn Asn Val Pro Cys Ser 1 5 10 <210> 2719 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2719 Phe Glu Gly Arg Arg Asn Arg Arg Arg Arg 1 5 10 <210> 2720 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2720 Ile Asn Val Lys Val Gly Gly Asn Ser Lys 1 5 10 <210> 2721 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2721 Ala Ser Asp Pro Leu Asp Thr Leu Gly Ser 1 5 10 <210> 2722 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2722 Leu Gln Asp Val Pro Arg Gly Gln Val Val 1 5 10 <210> 2723 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2723 Val Ala Ala Pro Pro Ser Gly Gly Pro Gly 1 5 10 <210> 2724 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2724 Asp Thr Leu Asn Leu Asn Leu Arg Ala Val 1 5 10 <210> 2725 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2725 Val Gly Val Gln Leu Gln Asp Val Pro Arg 1 5 10 <210> 2726 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2726 Arg Arg Arg Arg Glu Ala Pro Lys Val Val 1 5 10 <210> 2727 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2727 Arg Arg Arg Arg Glu Ala Pro Lys Val Val 1 5 10 <210> 2728 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2728 Val Gly Val Gln Leu Gln Asp Val Pro Arg 1 5 10 <210> 2729 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2729 Arg Arg Arg Arg Glu Ala Pro Lys Val Val 1 5 10 <210> 2730 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2730 Gly Ser Val Phe Leu Arg Asn Pro Ser Arg 1 5 10 <210> 2731 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2731 Val Pro Leu Ser Val Gly Val Gln Leu Gln 1 5 10 <210> 2732 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2732 Asp Thr Leu Asn Leu Asn Leu Arg Ala Val 1 5 10 <210> 2733 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2733 Arg Ala Arg Pro Ala Lys Ala Ala Ala Thr 1 5 10 <210> 2734 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2734 Arg Ala Arg Pro Ala Lys Ala Ala Ala Thr 1 5 10 <210> 2735 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2735 Arg Ala Arg Pro Ala Lys Ala Ala Ala Thr 1 5 10 <210> 2736 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2736 Arg Ala Arg Pro Ala Lys Ala Ala Ala Thr 1 5 10 <210> 2737 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2737 Gly His Arg Pro Leu Asp Lys Lys Arg Glu 1 5 10 <210> 2738 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2738 Arg Pro Leu Asp Lys Lys Arg Glu Glu Ala 1 5 10 <210> 2739 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2739 Arg Gly His Arg Pro Leu Asp Lys Lys Arg 1 5 10 <210> 2740 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2740 Glu Ala Pro Ser Leu Arg Pro Ala Pro Pro 1 5 10 <210> 2741 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2741 Arg Ala Arg Pro Ala Lys Ala Ala Ala Thr 1 5 10 <210> 2742 <211> 9 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2742 Ala Arg Pro Ala Lys Ala Ala Ala Thr 1 5 <210> 2743 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2743 Lys Lys Arg Glu Glu Ala Pro Ser Leu Arg 1 5 10 <210> 2744 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2744 Arg Ala Arg Pro Ala Lys Ala Ala Ala Thr 1 5 10 <210> 2745 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2745 Glu Glu Ala Pro Ser Leu Arg Pro Ala Pro 1 5 10 <210> 2746 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2746 Arg Gly His Arg Pro Leu Asp Lys Lys Arg 1 5 10 <210> 2747 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2747 Ala Ala Ala Thr Gln Lys Lys Val Glu Arg 1 5 10 <210> 2748 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2748 Ala Arg Gly His Arg Pro Leu Asp Lys Lys 1 5 10 <210> 2749 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2749 Lys Lys Arg Glu Glu Ala Pro Ser Leu Arg 1 5 10 <210> 2750 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2750 Ala Arg Pro Ala Lys Ala Ala Ala Thr Gln 1 5 10 <210> 2751 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2751 Lys Arg Glu Glu Ala Pro Ser Leu Arg Pro 1 5 10 <210> 2752 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2752 Arg Pro Ala Pro Pro Pro Ile Ser Gly Gly 1 5 10 <210> 2753 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2753 Leu Arg Pro Ala Pro Pro Pro Ile Ser Gly 1 5 10 <210> 2754 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2754 Arg Glu Glu Ala Pro Ser Leu Arg Pro Ala 1 5 10 <210> 2755 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2755 Arg Gly His Arg Pro Leu Asp Lys Lys Arg 1 5 10 <210> 2756 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2756 Ala Arg Pro Ala Lys Ala Ala Ala Thr Gln 1 5 10 <210> 2757 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2757 Arg Ala Arg Pro Ala Lys Ala Ala Ala Thr 1 5 10 <210> 2758 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2758 Lys Lys Arg Glu Glu Ala Pro Ser Leu Arg 1 5 10 <210> 2759 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2759 Ala Lys Ala Ala Ala Thr Gln Lys Lys Val 1 5 10 <210> 2760 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2760 Ala Thr Gln Lys Lys Val Glu Arg Lys Ala 1 5 10 <210> 2761 <211> 8 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2761 Ile Arg Pro Phe Phe Pro Gln Gln 1 5 <210> 2762 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2762 Arg Gly His Arg Pro Leu Asp Lys Lys Arg 1 5 10 <210> 2763 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2763 Gly Gly Gly Tyr Arg Ala Arg Pro Ala Lys 1 5 10 <210> 2764 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2764 Ala Pro Ser Leu Arg Pro Ala Pro Pro Pro 1 5 10 <210> 2765 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2765 Lys Ala Ala Ala Thr Gln Lys Lys Val Glu 1 5 10 <210> 2766 <211> 37 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2766 Phe Phe Gly His Gly Ala Glu Asp Ser Leu Ala Asp Gln Ala Ala Asn 1 5 10 15 Glu Trp Gly Arg Ser Gly Lys Asp Pro Asn His Phe Arg Pro Ala Gly 20 25 30 Leu Pro Glu Lys Tyr 35 <210> 2767 <211> 47 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2767 Ile Ser Asp Ala Arg Glu Asn Ile Gln Arg Phe Phe Gly His Gly Ala 1 5 10 15 Glu Asp Ser Leu Ala Asp Gln Ala Ala Asn Glu Trp Gly Arg Ser Gly 20 25 30 Lys Asp Pro Asn His Phe Arg Pro Ala Gly Leu Pro Glu Lys Tyr 35 40 45 <210> 2768 <211> 29 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2768 Ser Leu Ala Asp Gln Ala Ala Asn Glu Trp Gly Arg Ser Gly Lys Asp 1 5 10 15 Pro Asn His Phe Arg Pro Ala Gly Leu Pro Glu Lys Tyr 20 25 <210> 2769 <211> 36 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2769 Phe Gly His Gly Ala Glu Asp Ser Leu Ala Asp Gln Ala Ala Asn Glu 1 5 10 15 Trp Gly Arg Ser Gly Lys Asp Pro Asn His Phe Arg Pro Ala Gly Leu 20 25 30 Pro Glu Lys Tyr 35 <210> 2770 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2770 Gly Ala Arg Asp Met Trp Arg Ala Tyr Ser 1 5 10 <210> 2771 <211> 13 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2771 Pro Asn His Phe Arg Pro Ala Gly Leu Pro Glu Lys Tyr 1 5 10 <210> 2772 <211> 50 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2772 Ala Glu Ala Ile Ser Asp Ala Arg Glu Asn Ile Gln Arg Phe Phe Gly 1 5 10 15 His Gly Ala Glu Asp Ser Leu Ala Asp Gln Ala Ala Asn Glu Trp Gly 20 25 30 Arg Ser Gly Lys Asp Pro Asn His Phe Arg Pro Ala Gly Leu Pro Glu 35 40 45 Lys Tyr 50 <210> 2773 <211> 23 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2773 Ala Asn Glu Trp Gly Arg Ser Gly Lys Asp Pro Asn His Phe Arg Pro 1 5 10 15 Ala Gly Leu Pro Glu Lys Tyr 20 <210> 2774 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2774 Gly Gly Val Trp Ala Ala Glu Ala Ile Ser 1 5 10 <210> 2775 <211> 44 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2775 Ala Arg Glu Asn Ile Gln Arg Phe Phe Gly His Gly Ala Glu Asp Ser 1 5 10 15 Leu Ala Asp Gln Ala Ala Asn Glu Trp Gly Arg Ser Gly Lys Asp Pro 20 25 30 Asn His Phe Arg Pro Ala Gly Leu Pro Glu Lys Tyr 35 40 <210> 2776 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2776 Gly Ala Arg Asp Met Trp Arg Ala Tyr Ser 1 5 10 <210> 2777 <211> 26 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2777 Asp Gln Ala Ala Asn Glu Trp Gly Arg Ser Gly Lys Asp Pro Asn His 1 5 10 15 Phe Arg Pro Ala Gly Leu Pro Glu Lys Tyr 20 25 <210> 2778 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2778 Gly Gly Val Trp Ala Ala Glu Val Ile Ser 1 5 10 <210> 2779 <211> 25 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2779 Gln Ala Ala Asn Glu Trp Gly Arg Ser Gly Lys Asp Pro Asn His Phe 1 5 10 15 Arg Pro Ala Gly Leu Pro Glu Lys Tyr 20 25 <210> 2780 <211> 38 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2780 Arg Phe Phe Gly His Gly Ala Glu Asp Ser Leu Ala Asp Gln Ala Ala 1 5 10 15 Asn Glu Trp Gly Arg Ser Gly Lys Asp Pro Asn His Phe Arg Pro Ala 20 25 30 Gly Leu Pro Glu Lys Tyr 35 <210> 2781 <211> 33 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2781 Gly Ala Glu Asp Ser Leu Ala Asp Gln Ala Ala Asn Glu Trp Gly Arg 1 5 10 15 Ser Gly Lys Asp Pro Asn His Phe Arg Pro Ala Gly Leu Pro Glu Lys 20 25 30 Tyr <210> 2782 <211> 14 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2782 Asp Pro Asn His Phe Arg Pro Ala Gly Leu Pro Glu Lys Tyr 1 5 10 <210> 2783 <211> 34 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2783 His Gly Ala Glu Asp Ser Leu Ala Asp Gln Ala Ala Asn Glu Trp Gly 1 5 10 15 Arg Ser Gly Lys Asp Pro Asn His Phe Arg Pro Ala Gly Leu Pro Glu 20 25 30 Lys Tyr <210> 2784 <211> 17 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2784 Ser Gly Lys Asp Pro Asn His Phe Arg Pro Ala Gly Leu Pro Glu Lys 1 5 10 15 Tyr <210> 2785 <211> 22 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2785 Asn Glu Trp Gly Arg Ser Gly Lys Asp Pro Asn His Phe Arg Pro Ala 1 5 10 15 Gly Leu Pro Glu Lys Tyr 20 <210> 2786 <211> 45 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2786 Asp Ala Arg Glu Asn Ile Gln Arg Phe Phe Gly His Gly Ala Glu Asp 1 5 10 15 Ser Leu Ala Asp Gln Ala Ala Asn Glu Trp Gly Arg Ser Gly Lys Asp 20 25 30 Pro Asn His Phe Arg Pro Ala Gly Leu Pro Glu Lys Tyr 35 40 45 <210> 2787 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2787 Gly Gly Val Trp Ala Ala Glu Ala Ile Ser 1 5 10 <210> 2788 <211> 6 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2788 Gly Leu Pro Glu Lys Tyr 1 5 <210> 2789 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2789 Ser Leu Ala Asp Gln Ala Ala Asn Glu Trp 1 5 10 <210> 2790 <211> 27 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2790 Ala Asp Gln Ala Ala Asn Glu Trp Gly Arg Ser Gly Lys Asp Pro Asn 1 5 10 15 His Phe Arg Pro Ala Gly Leu Pro Glu Lys Tyr 20 25 <210> 2791 <211> 46 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2791 Ser Asp Ala Arg Glu Asn Ile Gln Arg Phe Phe Gly His Gly Ala Glu 1 5 10 15 Asp Ser Leu Ala Asp Gln Ala Ala Asn Glu Trp Gly Arg Ser Gly Lys 20 25 30 Asp Pro Asn His Phe Arg Pro Ala Gly Leu Pro Glu Lys Tyr 35 40 45 <210> 2792 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2792 Gly Gly Val Trp Ala Ala Glu Ala Ile Ser 1 5 10 <210> 2793 <211> 65 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2793 Gly Asn Tyr Asp Ala Ala Lys Arg Gly Pro Gly Gly Val Trp Ala Ala 1 5 10 15 Glu Ala Ile Ser Asp Ala Arg Glu Asn Ile Gln Arg Phe Phe Gly His 20 25 30 Gly Ala Glu Asp Ser Leu Ala Asp Gln Ala Ala Asn Glu Trp Gly Arg 35 40 45 Ser Gly Lys Asp Pro Asn His Phe Arg Pro Ala Gly Leu Pro Glu Lys 50 55 60 Tyr 65 <210> 2794 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2794 Gly Glu Ala Phe Asp Gly Ala Arg Asp Met 1 5 10 <210> 2795 <211> 55 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2795 Gly Gly Val Trp Ala Ala Glu Ala Ile Ser Asp Ala Arg Glu Asn Ile 1 5 10 15 Gln Arg Phe Phe Gly His Gly Ala Glu Asp Ser Leu Ala Asp Gln Ala 20 25 30 Ala Asn Glu Trp Gly Arg Ser Gly Lys Asp Pro Asn His Phe Arg Pro 35 40 45 Ala Gly Leu Pro Glu Lys Tyr 50 55 <210> 2796 <211> 29 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2796 Asp Ser Gly Pro Arg Arg Tyr Thr Ile Ala Ala Leu Leu Ser Pro Tyr 1 5 10 15 Ser Tyr Ser Thr Thr Ala Val Val Thr Asn Pro Lys Glu 20 25 <210> 2797 <211> 27 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2797 Gly Pro Arg Arg Tyr Thr Ile Ala Ala Leu Leu Ser Pro Tyr Ser Tyr 1 5 10 15 Ser Thr Thr Ala Val Val Thr Asn Pro Lys Glu 20 25 <210> 2798 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2798 Ser Gly Pro Arg Arg Tyr Thr Ile Ala Ala Leu Leu Ser Pro Tyr Ser 1 5 10 15 Tyr Ser Thr Thr Ala Val Val Thr Asn Pro Lys Glu 20 25 <210> 2799 <211> 26 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2799 Pro Arg Arg Tyr Thr Ile Ala Ala Leu Leu Ser Pro Tyr Ser Tyr Ser 1 5 10 15 Thr Thr Ala Val Val Thr Asn Pro Lys Glu 20 25 <210> 2800 <211> 16 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2800 Ser Pro Tyr Ser Tyr Ser Thr Thr Ala Val Val Thr Asn Pro Lys Glu 1 5 10 15 <210> 2801 <211> 19 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2801 Ala Leu Leu Ser Pro Tyr Ser Tyr Ser Thr Thr Ala Val Val Thr Asn 1 5 10 15 Pro Lys Glu <210> 2802 <211> 21 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2802 Ile Ala Ala Leu Leu Ser Pro Tyr Ser Tyr Ser Thr Thr Ala Val Val 1 5 10 15 Thr Asn Pro Lys Glu 20 <210> 2803 <211> 32 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2803 Thr Ala Asn Asp Ser Gly Pro Arg Arg Tyr Thr Ile Ala Ala Leu Leu 1 5 10 15 Ser Pro Tyr Ser Tyr Ser Thr Thr Ala Val Val Thr Asn Pro Lys Glu 20 25 30 <210> 2804 <211> 44 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2804 Ile Ser Pro Phe His Glu His Ala Glu Val Val Phe Thr Ala Asn Asp 1 5 10 15 Ser Gly Pro Arg Arg Tyr Thr Ile Ala Ala Leu Leu Ser Pro Tyr Ser 20 25 30 Tyr Ser Thr Thr Ala Val Val Thr Asn Pro Lys Glu 35 40 <210> 2805 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2805 Ser Pro Pro Gly Val Cys Ser Arg Asp Pro 1 5 10 <210> 2806 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2806 Leu Gly Asn Gln Glu Pro Gly Gly Gln Thr 1 5 10 <210> 2807 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2807 Ser Pro Pro Gly Val Cys Ser Arg Asp Pro 1 5 10 <210> 2808 <211> 16 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2808 Leu Val Pro Pro Met Glu Asp Tyr Pro Gln Phe Gly Ser Pro Lys 1 5 10 15 <210> 2809 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2809 Leu Gly Asn Gln Glu Pro Gly Gly Gln Thr 1 5 10 <210> 2810 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2810 Asn Gln Glu Gln Val Ser Pro Leu Thr Leu 1 5 10 <210> 2811 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2811 Asn Gln Glu Gln Val Ser Pro Leu Thr Leu 1 5 10 <210> 2812 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2812 Leu Gly Asn Gln Glu Pro Gly Gly Gln Thr 1 5 10 <210> 2813 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2813 Asn Gln Glu Pro Gly Gly Gln Thr Ala Leu 1 5 10 <210> 2814 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2814 Asp Ser Pro Gly Asn Lys Asp Phe Leu Gln 1 5 10 <210> 2815 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2815 Leu Lys Leu Gly Asn Gln Glu Pro Gly Gly 1 5 10 <210> 2816 <211> 22 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2816 Leu Glu Ser Phe Lys Val Ser Phe Leu Ser Ala Leu Glu Glu Tyr Thr 1 5 10 15 Lys Lys Leu Asn Thr Gln 20 <210> 2817 <211> 21 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2817 Glu Ser Phe Lys Val Ser Phe Leu Ser Ala Leu Glu Glu Tyr Thr Lys 1 5 10 15 Lys Leu Asn Thr Gln 20 <210> 2818 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2818 Asn Leu Lys Leu Leu Asp Asn Trp Asp Ser 1 5 10 <210> 2819 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2819 Asp Ser Gly Arg Asp Tyr Val Ser Gln Phe 1 5 10 <210> 2820 <211> 20 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2820 Ser Phe Lys Val Ser Phe Leu Ser Ala Leu Glu Glu Tyr Thr Lys Lys 1 5 10 15 Leu Asn Thr Gln 20 <210> 2821 <211> 17 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2821 Val Ser Phe Leu Ser Ala Leu Glu Glu Tyr Thr Lys Lys Leu Asn Thr 1 5 10 15 Gln <210> 2822 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2822 Ser Lys Asp Leu Glu Glu Val Lys Ala Lys 1 5 10 <210> 2823 <211> 13 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2823 Ser Ala Leu Glu Glu Tyr Thr Lys Lys Leu Asn Thr Gln 1 5 10 <210> 2824 <211> 16 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2824 Ser Phe Leu Ser Ala Leu Glu Glu Tyr Thr Lys Lys Leu Asn Thr Gln 1 5 10 15 <210> 2825 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2825 Leu Ala Thr Val Tyr Val Asp Val Leu Lys 1 5 10 <210> 2826 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2826 Glu Lys Leu Ser Pro Leu Gly Glu Glu Met 1 5 10 <210> 2827 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2827 Glu Glu Met Arg Asp Arg Ala Arg Ala His 1 5 10 <210> 2828 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2828 Val Asp Val Leu Lys Asp Ser Gly Arg Asp 1 5 10 <210> 2829 <211> 38 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2829 Leu Val Glu Thr Arg Thr Ile Val Arg Phe Asn Arg Pro Phe Leu Met 1 5 10 15 Ile Ile Val Pro Thr Asp Thr Gln Asn Ile Phe Phe Met Ser Lys Val 20 25 30 Thr Asn Pro Lys Gln Ala 35 <210> 2830 <211> 40 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2830 Ser Ala Leu Val Glu Thr Arg Thr Ile Val Arg Phe Asn Arg Pro Phe 1 5 10 15 Leu Met Ile Ile Val Pro Thr Asp Thr Gln Asn Ile Phe Phe Met Ser 20 25 30 Lys Val Thr Asn Pro Lys Gln Ala 35 40 <210> 2831 <211> 37 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2831 Val Glu Thr Arg Thr Ile Val Arg Phe Asn Arg Pro Phe Leu Met Ile 1 5 10 15 Ile Val Pro Thr Asp Thr Gln Asn Ile Phe Phe Met Ser Lys Val Thr 20 25 30 Asn Pro Lys Gln Ala 35 <210> 2832 <211> 35 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2832 Thr Arg Thr Ile Val Arg Phe Asn Arg Pro Phe Leu Met Ile Ile Val 1 5 10 15 Pro Thr Asp Thr Gln Asn Ile Phe Phe Met Ser Lys Val Thr Asn Pro 20 25 30 Lys Gln Ala 35 <210> 2833 <211> 16 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2833 Thr Gln Asn Ile Phe Phe Met Ser Lys Val Thr Asn Pro Lys Gln Ala 1 5 10 15 <210> 2834 <211> 39 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2834 Ala Leu Val Glu Thr Arg Thr Ile Val Arg Phe Asn Arg Pro Phe Leu 1 5 10 15 Met Ile Ile Val Pro Thr Asp Thr Gln Asn Ile Phe Phe Met Ser Lys 20 25 30 Val Thr Asn Pro Lys Gln Ala 35 <210> 2835 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2835 Gln Glu Asn Gln Asp Arg Gly Thr His Val 1 5 10 <210> 2836 <211> 22 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2836 Ile Ile Val Pro Thr Asp Thr Gln Asn Ile Phe Phe Met Ser Lys Val 1 5 10 15 Thr Asn Pro Lys Gln Ala 20 <210> 2837 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2837 Ser Ala Asn Val Asp Phe Ala Phe Ser Leu 1 5 10 <210> 2838 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2838 Lys Arg His Ser Gln Gly Thr Phe Thr Ser 1 5 10 <210> 2839 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2839 Asp Lys Arg His Ser Gln Gly Thr Phe Thr 1 5 10 <210> 2840 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2840 Lys Arg His Ser Gln Gly Thr Phe Thr Ser 1 5 10 <210> 2841 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2841 Lys Arg His Ser Gln Gly Thr Phe Thr Ser 1 5 10 <210> 2842 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2842 Phe Val Gln Trp Leu Met Asn Thr Lys Arg 1 5 10 <210> 2843 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2843 Asp Lys Arg His Ser Gln Gly Thr Phe Thr 1 5 10 <210> 2844 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2844 Lys Arg Asn Arg Asn Asn Ile Ala Lys Arg 1 5 10 <210> 2845 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2845 Lys Arg His Ser Gln Gly Thr Phe Thr Ser 1 5 10 <210> 2846 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2846 Asp Lys Arg His Ser Gln Gly Thr Phe Thr 1 5 10 <210> 2847 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2847 Arg Arg Asp Phe Pro Glu Glu Val Ala Ile 1 5 10 <210> 2848 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2848 Arg Arg Arg Arg Arg Asp Thr His Phe Pro 1 5 10 <210> 2849 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2849 Phe Gln Arg Arg Arg Arg Arg Asp Thr His 1 5 10 <210> 2850 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2850 Met Phe Gln Arg Arg Arg Arg Arg Asp Thr 1 5 10 <210> 2851 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2851 Ser Trp Met Pro Met Phe Gln Arg Arg Arg 1 5 10 <210> 2852 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2852 Trp Met Pro Met Phe Gln Arg Arg Arg Arg 1 5 10 <210> 2853 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2853 Arg Ala Ser Trp Met Pro Met Phe Gln Arg 1 5 10 <210> 2854 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2854 Trp Met Pro Met Phe Gln Arg Arg Arg Arg 1 5 10 <210> 2855 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2855 Trp Met Pro Met Phe Gln Arg Arg Arg Arg 1 5 10 <210> 2856 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2856 Arg Ala Ser Trp Met Pro Met Phe Gln Arg 1 5 10 <210> 2857 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2857 Leu Gln Pro Gln Asp Arg Ala Gly Ala Arg 1 5 10 <210> 2858 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2858 Ala Ser Trp Met Pro Met Phe Gln Arg Arg 1 5 10 <210> 2859 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2859 Gln Asp Arg Ala Gly Ala Arg Ala Ser Trp 1 5 10 <210> 2860 <211> 37 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2860 Leu Thr Gly Arg Gly Ala Glu Asp Ser Leu Ala Asp Gln Ala Ala Asn 1 5 10 15 Lys Trp Gly Arg Ser Gly Arg Asp Pro Asn His Phe Arg Pro Ala Gly 20 25 30 Leu Pro Glu Lys Tyr 35 <210> 2861 <211> 36 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2861 Thr Gly Arg Gly Ala Glu Asp Ser Leu Ala Asp Gln Ala Ala Asn Lys 1 5 10 15 Trp Gly Arg Ser Gly Arg Asp Pro Asn His Phe Arg Pro Ala Gly Leu 20 25 30 Pro Glu Lys Tyr 35 <210> 2862 <211> 14 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2862 Asp Pro Asn His Phe Arg Pro Ala Gly Leu Pro Glu Lys Tyr 1 5 10 <210> 2863 <211> 35 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2863 Gly Arg Gly Ala Glu Asp Ser Leu Ala Asp Gln Ala Ala Asn Lys Trp 1 5 10 15 Gly Arg Ser Gly Arg Asp Pro Asn His Phe Arg Pro Ala Gly Leu Pro 20 25 30 Glu Lys Tyr 35 <210> 2864 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2864 Phe Arg Pro Ala Gly Leu Pro Glu Lys Tyr 1 5 10 <210> 2865 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2865 Phe Arg Pro Ala Gly Leu Pro Glu Lys Tyr 1 5 10 <210> 2866 <211> 29 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2866 Ser Leu Ala Asp Gln Ala Ala Asn Lys Trp Gly Arg Ser Gly Arg Asp 1 5 10 15 Pro Asn His Phe Arg Pro Ala Gly Leu Pro Glu Lys Tyr 20 25 <210> 2867 <211> 34 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2867 Arg Gly Ala Glu Asp Ser Leu Ala Asp Gln Ala Ala Asn Lys Trp Gly 1 5 10 15 Arg Ser Gly Arg Asp Pro Asn His Phe Arg Pro Ala Gly Leu Pro Glu 20 25 30 Lys Tyr <210> 2868 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2868 Phe Arg Pro Ala Gly Leu Pro Glu Lys Tyr 1 5 10 <210> 2869 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2869 Ser Asn Ala Arg Glu Asn Ile Gln Arg Leu 1 5 10 <210> 2870 <211> 50 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2870 Ala Glu Val Ile Ser Asn Ala Arg Glu Asn Ile Gln Arg Leu Thr Gly 1 5 10 15 Arg Gly Ala Glu Asp Ser Leu Ala Asp Gln Ala Ala Asn Lys Trp Gly 20 25 30 Arg Ser Gly Arg Asp Pro Asn His Phe Arg Pro Ala Gly Leu Pro Glu 35 40 45 Lys Tyr 50 <210> 2871 <211> 26 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2871 Asp Gln Ala Ala Asn Lys Trp Gly Arg Ser Gly Arg Asp Pro Asn His 1 5 10 15 Phe Arg Pro Ala Gly Leu Pro Glu Lys Tyr 20 25 <210> 2872 <211> 49 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2872 Glu Val Ile Ser Asn Ala Arg Glu Asn Ile Gln Arg Leu Thr Gly Arg 1 5 10 15 Gly Ala Glu Asp Ser Leu Ala Asp Gln Ala Ala Asn Lys Trp Gly Arg 20 25 30 Ser Gly Arg Asp Pro Asn His Phe Arg Pro Ala Gly Leu Pro Glu Lys 35 40 45 Tyr <210> 2873 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2873 Lys Lys Thr Glu Thr Gln Glu Lys Asn Pro 1 5 10 <210> 2874 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2874 Thr Gln Glu Lys Asn Pro Leu Pro Ser Lys 1 5 10 <210> 2875 <211> 21 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2875 Gln Glu Lys Asn Pro Leu Pro Ser Lys Glu Thr Ile Glu Gln Glu Lys 1 5 10 15 Gln Ala Gly Glu Ser 20 <210> 2876 <211> 43 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2876 Ser Asp Lys Pro Asp Met Ala Glu Ile Glu Lys Phe Asp Lys Ser Lys 1 5 10 15 Leu Lys Lys Thr Glu Thr Gln Glu Lys Asn Pro Leu Pro Ser Lys Glu 20 25 30 Thr Ile Glu Gln Glu Lys Gln Ala Gly Glu Ser 35 40 <210> 2877 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2877 Lys Asn Pro Leu Pro Ser Lys Glu Thr Ile 1 5 10 <210> 2878 <211> 22 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2878 Thr Gln Glu Lys Asn Pro Leu Pro Ser Lys Glu Thr Ile Glu Gln Glu 1 5 10 15 Lys Gln Ala Gly Glu Ser 20 <210> 2879 <211> 19 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2879 Lys Asn Pro Leu Pro Ser Lys Glu Thr Ile Glu Gln Glu Lys Gln Ala 1 5 10 15 Gly Glu Ser <210> 2880 <211> 24 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2880 Thr Glu Thr Gln Glu Lys Asn Pro Leu Pro Ser Lys Glu Thr Ile Glu 1 5 10 15 Gln Glu Lys Gln Ala Gly Glu Ser 20 <210> 2881 <211> 20 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2881 Glu Lys Asn Pro Leu Pro Ser Lys Glu Thr Ile Glu Gln Glu Lys Gln 1 5 10 15 Ala Gly Glu Ser 20 <210> 2882 <211> 18 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2882 Asn Pro Leu Pro Ser Lys Glu Thr Ile Glu Gln Glu Lys Gln Ala Gly 1 5 10 15 Glu Ser <210> 2883 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2883 His Asn Leu Thr Thr Gly Ala Thr Leu Ile 1 5 10 <210> 2884 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2884 Asn Leu Thr Thr Gly Ala Thr Leu Ile Asn 1 5 10 <210> 2885 <211> 16 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2885 Lys Val Thr Ser Ile Gln Asp Trp Val Gln Lys Thr Ile Ala Glu Asn 1 5 10 15 <210> 2886 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2886 Ser His His Asn Leu Thr Thr Gly Ala Thr 1 5 10 <210> 2887 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2887 Ala Lys Met Val Ser His His Asn Leu Thr 1 5 10 <210> 2888 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2888 Leu Phe Ala Val Asp Ser Gly Asn Asp Val 1 5 10 <210> 2889 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2889 Leu Phe Ala Val Asp Ser Gly Asn Asp Val 1 5 10 <210> 2890 <211> 35 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2890 Val Thr Leu Ala Ala His Leu Pro Ala Glu Phe Thr Pro Ala Val His 1 5 10 15 Ala Ser Leu Asp Lys Phe Leu Ala Ser Val Ser Thr Val Leu Thr Ser 20 25 30 Lys Tyr Arg 35 <210> 2891 <211> 33 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2891 Leu Ala Ala His Leu Pro Ala Glu Phe Thr Pro Ala Val His Ala Ser 1 5 10 15 Leu Asp Lys Phe Leu Ala Ser Val Ser Thr Val Leu Thr Ser Lys Tyr 20 25 30 Arg <210> 2892 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2892 Phe Leu Ser Phe Pro Thr Thr Lys Thr Tyr 1 5 10 <210> 2893 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2893 Leu Ser Phe Pro Thr Thr Lys Thr Tyr Phe 1 5 10 <210> 2894 <211> 15 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2894 Lys Phe Leu Ala Ser Val Ser Thr Val Leu Thr Ser Lys Tyr Arg 1 5 10 15 <210> 2895 <211> 32 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2895 Ala Ala His Leu Pro Ala Glu Phe Thr Pro Ala Val His Ala Ser Leu 1 5 10 15 Asp Lys Phe Leu Ala Ser Val Ser Thr Val Leu Thr Ser Lys Tyr Arg 20 25 30 <210> 2896 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2896 Pro Thr Thr Lys Thr Tyr Phe Pro His Phe 1 5 10 <210> 2897 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2897 Ala His Ala Gly Glu Tyr Gly Ala Glu Ala 1 5 10 <210> 2898 <211> 31 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2898 Tyr Glu Gly Ser Tyr Ala Leu Thr Ser Glu Glu Ala Glu Arg Ser Asp 1 5 10 15 Gly Asp Pro Val Gln Pro Ala Val Leu Gln Val His Gln Thr Ser 20 25 30 <210> 2899 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2899 Gln Glu Lys Pro Ser Ser Pro Ser Pro Met 1 5 10 <210> 2900 <211> 26 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2900 Ala Leu Thr Ser Glu Glu Ala Glu Arg Ser Asp Gly Asp Pro Val Gln 1 5 10 15 Pro Ala Val Leu Gln Val His Gln Thr Ser 20 25 <210> 2901 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2901 Ser Asp Met Arg Gln Glu Lys Pro Ser Ser 1 5 10 <210> 2902 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2902 Arg Gln Glu Lys Pro Ser Ser Pro Ser Pro 1 5 10 <210> 2903 <211> 28 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2903 Ser Tyr Ala Leu Thr Ser Glu Glu Ala Glu Arg Ser Asp Gly Asp Pro 1 5 10 15 Val Gln Pro Ala Val Leu Gln Val His Gln Thr Ser 20 25 <210> 2904 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2904 Ala Ala Pro Pro Gly His Gln Leu His Arg 1 5 10 <210> 2905 <211> 27 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2905 Thr Val Val Gln Pro Ser Val Gly Ala Ala Ala Gly Pro Val Val Pro 1 5 10 15 Pro Cys Pro Gly Arg Ile Arg His Phe Lys Val 20 25 <210> 2906 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2906 Ala Pro Pro Gly His Gln Leu His Arg Ala 1 5 10 <210> 2907 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2907 Arg Thr Val Val Gln Pro Ser Val Gly Ala 1 5 10 <210> 2908 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2908 Arg Thr Val Val Gln Pro Ser Val Gly Ala 1 5 10 <210> 2909 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2909 Arg Thr Val Val Gln Pro Ser Val Gly Ala 1 5 10 <210> 2910 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2910 Leu Ala Ala Pro Pro Gly His Gln Leu His 1 5 10 <210> 2911 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2911 Lys Thr Arg Thr Val Val Gln Pro Ser Val 1 5 10 <210> 2912 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2912 Glu Lys Arg Glu Asp Ser Lys Glu Ala Glu 1 5 10 <210> 2913 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2913 Lys Arg Glu Asp Ser Lys Glu Ala Glu Lys 1 5 10 <210> 2914 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2914 Glu Lys Arg Glu Asp Ser Lys Glu Ala Glu 1 5 10 <210> 2915 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2915 Arg Arg Gly Trp Arg Pro Ser Ser Arg Glu 1 5 10 <210> 2916 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2916 Arg Ala Arg Ala Tyr Gly Phe Arg Gly Pro 1 5 10 <210> 2917 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2917 Ser Glu Glu Thr Lys Glu Asn Glu Gly Phe 1 5 10 <210> 2918 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2918 Arg Ser Glu Glu Thr Lys Glu Asn Glu Gly 1 5 10 <210> 2919 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2919 Arg Ser Glu Glu Thr Lys Glu Asn Glu Gly 1 5 10 <210> 2920 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2920 Arg Ser Glu Glu Thr Lys Glu Asn Glu Gly 1 5 10 <210> 2921 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2921 Gly Asp Val Pro Val Thr Val Thr Val His 1 5 10 <210> 2922 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2922 Arg Ser Glu Glu Thr Lys Glu Asn Glu Gly 1 5 10 <210> 2923 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2923 Arg Ser Glu Glu Thr Lys Glu Asn Glu Gly 1 5 10 <210> 2924 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2924 Arg Ser Glu Glu Thr Lys Glu Asn Glu Gly 1 5 10 <210> 2925 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2925 Arg Ser Glu Glu Thr Lys Glu Asn Glu Gly 1 5 10 <210> 2926 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2926 Lys Lys Gln Arg Phe Arg His Arg Asn Arg 1 5 10 <210> 2927 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2927 Gly Met Ala Pro Arg Pro Ser Leu Ala Lys 1 5 10 <210> 2928 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2928 Ile Asp Ser Arg Pro Glu Thr Leu His Pro 1 5 10 <210> 2929 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2929 Lys Lys Gln Arg Phe Arg His Arg Asn Arg 1 5 10 <210> 2930 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2930 Ser Leu Ala Lys Lys Gln Arg Phe Arg His 1 5 10 <210> 2931 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2931 Lys Lys Gln Arg Phe Arg His Arg Asn Arg 1 5 10 <210> 2932 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2932 Leu Ala Lys Lys Gln Arg Phe Arg His Arg 1 5 10 <210> 2933 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2933 Asp Glu Phe Pro Gly Ile Pro Ser Pro Leu 1 5 10 <210> 2934 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2934 Lys Glu Lys Gly Tyr Pro Lys Leu Leu Gln 1 5 10 <210> 2935 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2935 Lys Gly Tyr Pro Lys Leu Leu Gln Asp Glu 1 5 10 <210> 2936 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2936 Ser Val Phe Leu Ile Lys Gly Asp Lys Val 1 5 10 <210> 2937 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2937 Lys Lys Glu Lys Gly Tyr Pro Lys Leu Leu 1 5 10 <210> 2938 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2938 Asp Glu Phe Pro Gly Ile Pro Ser Pro Leu 1 5 10 <210> 2939 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2939 Gln Pro Val Ser Leu Ala Asn Thr Gln Pro 1 5 10 <210> 2940 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2940 Lys Phe Ser Pro Gly Ala Pro Gly Gly Ser 1 5 10 <210> 2941 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2941 Ser Gln Thr Gln Pro Val Ser Leu Ala Asn 1 5 10 <210> 2942 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2942 Tyr Ala Pro Gln Lys Lys Phe Gly Pro Val 1 5 10 <210> 2943 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2943 Leu Ala Asn Thr Gln Pro Arg Gly Pro Pro 1 5 10 <210> 2944 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2944 Met Gly Arg Val Gly Glu Ile Pro Pro Pro 1 5 10 <210> 2945 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2945 Ala Leu Ser Ser Val Gln Glu Ser Gln Val 1 5 10 <210> 2946 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2946 Lys Asp Ala Leu Ser Ser Val Gln Glu Ser 1 5 10 <210> 2947 <211> 15 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2947 Trp Asp Leu Asp Pro Glu Val Arg Pro Thr Ser Ala Val Ala Ala 1 5 10 15 <210> 2948 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2948 Arg Gly Trp Val Thr Asp Gly Phe Ser Ser 1 5 10 <210> 2949 <211> 11 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2949 Pro Glu Val Arg Pro Thr Ser Ala Val Ala Ala 1 5 10 <210> 2950 <211> 7 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2950 Lys Arg Ala Met Glu Asn Met 1 5 <210> 2951 <211> 7 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2951 Lys Arg Ala Met Glu Asn Met 1 5 <210> 2952 <211> 9 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2952 Ile Ala Lys Arg Ala Met Glu Asn Met 1 5 <210> 2953 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2953 Lys Arg Phe Pro Val Gly Pro Pro Lys Asn 1 5 10 <210> 2954 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2954 Lys Arg Phe Pro Val Gly Pro Pro Lys Asn 1 5 10 <210> 2955 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2955 Val Glu Asp Ile Leu Asn Leu Leu Gly Met 1 5 10 <210> 2956 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2956 Glu Asn Ser Arg Asp Asn Pro Phe Lys Arg 1 5 10 <210> 2957 <211> 38 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2957 Lys Pro Glu Val Leu Glu Val Thr Leu Asn Arg Pro Phe Leu Phe Ala 1 5 10 15 Val Tyr Asp Gln Ser Ala Thr Ala Leu His Phe Leu Gly Arg Val Ala 20 25 30 Asn Pro Leu Ser Thr Ala 35 <210> 2958 <211> 44 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2958 Ser Thr Gln Gln Leu Asn Lys Pro Glu Val Leu Glu Val Thr Leu Asn 1 5 10 15 Arg Pro Phe Leu Phe Ala Val Tyr Asp Gln Ser Ala Thr Ala Leu His 20 25 30 Phe Leu Gly Arg Val Ala Asn Pro Leu Ser Thr Ala 35 40 <210> 2959 <211> 42 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2959 Gln Gln Leu Asn Lys Pro Glu Val Leu Glu Val Thr Leu Asn Arg Pro 1 5 10 15 Phe Leu Phe Ala Val Tyr Asp Gln Ser Ala Thr Ala Leu His Phe Leu 20 25 30 Gly Arg Val Ala Asn Pro Leu Ser Thr Ala 35 40 <210> 2960 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2960 Ala Pro Leu Thr Lys Pro Leu Lys Ala Phe 1 5 10 <210> 2961 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2961 Lys Pro Leu Lys Ala Phe Thr Val Cys Leu 1 5 10 <210> 2962 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2962 Leu Lys Ala Pro Leu Thr Lys Pro Leu Lys 1 5 10 <210> 2963 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2963 Gln Cys Pro Phe Glu Asp His Val Lys Leu 1 5 10 <210> 2964 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2964 Ala Leu Val Leu Ile Ala Phe Ala Gln Tyr 1 5 10 <210> 2965 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2965 Ile Ala Phe Ala Gln Tyr Leu Gln Gln Cys 1 5 10 <210> 2966 <211> 21 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2966 Gly Thr Asn Arg Gly Ala Ser Gln Ala Gly Met Thr Gly Tyr Gly Met 1 5 10 15 Pro Arg Gln Ile Leu 20 <210> 2967 <211> 22 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2967 Met Gly Thr Asn Arg Gly Ala Ser Gln Ala Gly Met Thr Gly Tyr Gly 1 5 10 15 Met Pro Arg Gln Ile Leu 20 <210> 2968 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2968 Thr Gly Tyr Gly Met Pro Arg Gln Ile Leu 1 5 10 <210> 2969 <211> 7 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2969 Glu Leu Ser Pro Leu Asp Leu 1 5 <210> 2970 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2970 Ile Asn Met Leu Thr Arg Pro Arg Tyr Gly 1 5 10 <210> 2971 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2971 Gly Lys Arg His Lys Glu Asp Thr Leu Ala 1 5 10 <210> 2972 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2972 Gly Lys Arg His Lys Glu Asp Thr Leu Ala 1 5 10 <210> 2973 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2973 Arg Asn Ser Glu Pro Gln Asp Glu Gly Glu 1 5 10 <210> 2974 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2974 Arg Gly Ala Arg Asn Ser Glu Pro Gln Asp 1 5 10 <210> 2975 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2975 Arg Asn Ser Glu Pro Gln Asp Glu Gly Glu 1 5 10 <210> 2976 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2976 Arg Ser Pro Gln Pro Pro Pro Pro Ala Pro 1 5 10 <210> 2977 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2977 Arg Ser Pro Gln Pro Pro Pro Pro Ala Pro 1 5 10 <210> 2978 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2978 Arg Gly Ala Arg Asn Ser Glu Pro Gln Asp 1 5 10 <210> 2979 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2979 Val Arg Ser Gln Thr His Ser Leu Pro Ala 1 5 10 <210> 2980 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2980 Trp Asn Glu Val Leu Pro Pro Trp Asp Arg 1 5 10 <210> 2981 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2981 Ser Asp His Gly Glu Lys Lys Leu Ile Ser 1 5 10 <210> 2982 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2982 Asn Asn Pro Ala Gly Leu Tyr Ser Ser Glu 1 5 10 <210> 2983 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2983 Lys Val Ala Ala Ser Ile Gly Asn Ala Gln 1 5 10 <210> 2984 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2984 Ala Asn Ser Arg Pro Leu Asp His Ala Gln 1 5 10 <210> 2985 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2985 Leu Ser Val Ala Glu Ile Thr Asn Ala Cys 1 5 10 <210> 2986 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2986 Ser Val Ala Glu Ile Thr Asn Ala Cys Phe 1 5 10 <210> 2987 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2987 Ala Cys Phe Glu Pro Ala Asn Gln Met Val 1 5 10 <210> 2988 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2988 Leu Val Val Tyr Pro Trp Thr Gln Arg Phe 1 5 10 <210> 2989 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2989 Phe Glu Ser Phe Gly Asp Leu Ser Thr Pro 1 5 10 <210> 2990 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2990 Phe Glu Ser Phe Gly Asp Leu Ser Thr Pro 1 5 10 <210> 2991 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2991 Glu Thr Tyr Leu Ser Arg Gly Asp Ser Ser 1 5 10 <210> 2992 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2992 Glu Thr Tyr Leu Ser Arg Gly Asp Ser Ser 1 5 10 <210> 2993 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2993 Arg Glu Thr Tyr Leu Ser Arg Gly Asp Ser 1 5 10 <210> 2994 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2994 Glu Thr Tyr Leu Ser Arg Gly Asp Ser Ser 1 5 10 <210> 2995 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2995 Arg Ser Leu Pro Gly Glu Ser Glu Glu Met 1 5 10 <210> 2996 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2996 Asp Ala Pro Pro Gln Asp Pro Ser Cys Cys 1 5 10 <210> 2997 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2997 Ser Arg Lys Asn Pro Lys Phe Met Glu Thr 1 5 10 <210> 2998 <211> 20 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2998 Phe Met Glu Thr Val Ala Glu Lys Ala Leu Gln Glu Tyr Arg Lys Lys 1 5 10 15 His Arg Glu Glu 20 <210> 2999 <211> 57 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 2999 Thr Pro Asp Val Ser Ser Ala Leu Asp Lys Leu Lys Glu Phe Gly Asn 1 5 10 15 Thr Leu Glu Asp Lys Ala Arg Glu Leu Ile Ser Arg Ile Lys Gln Ser 20 25 30 Glu Leu Ser Ala Lys Met Arg Glu Trp Phe Ser Glu Thr Phe Gln Lys 35 40 45 Val Lys Glu Lys Leu Lys Ile Asp Ser 50 55 <210> 3000 <211> 55 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3000 Asp Val Ser Ser Ala Leu Asp Lys Leu Lys Glu Phe Gly Asn Thr Leu 1 5 10 15 Glu Asp Lys Ala Arg Glu Leu Ile Ser Arg Ile Lys Gln Ser Glu Leu 20 25 30 Ser Ala Lys Met Arg Glu Trp Phe Ser Glu Thr Phe Gln Lys Val Lys 35 40 45 Glu Lys Leu Lys Ile Asp Ser 50 55 <210> 3001 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3001 Ser Arg Lys Met Leu Glu Glu Ile Met Lys 1 5 10 <210> 3002 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3002 Thr Gln Ser Ala Ile Pro Tyr Ala Leu Arg 1 5 10 <210> 3003 <211> 18 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3003 Ile Gly Glu Gly Gln Gln His His Leu Gly Gly Ala Lys Gln Ala Gly 1 5 10 15 Asp Val <210> 3004 <211> 13 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3004 Glu Pro Pro Pro Arg Thr Leu Pro Ala Thr Asp Leu Gln 1 5 10 <210> 3005 <211> 12 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3005 Pro Pro Pro Arg Thr Leu Pro Ala Thr Asp Leu Gln 1 5 10 <210> 3006 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3006 Val Ala Pro Gly Gln Thr Ala Arg Ile Thr 1 5 10 <210> 3007 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3007 Val Ala Pro Gly Gln Thr Ala Arg Ile Thr 1 5 10 <210> 3008 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3008 Arg Lys Ser Ala Gly Ala Ala Lys Arg Lys 1 5 10 <210> 3009 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3009 Lys Lys Lys Ala Arg Lys Ser Ala Gly Ala 1 5 10 <210> 3010 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3010 Lys Lys Ala Arg Lys Ser Ala Gly Ala Ala 1 5 10 <210> 3011 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3011 Gln Leu Asp Ala Arg Asn Thr Lys Val Leu 1 5 10 <210> 3012 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3012 Arg Asn Thr Lys Val Leu Thr Phe Ile Ser 1 5 10 <210> 3013 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3013 Val Ser Pro Gly Gln Thr Ala Arg Ile Thr 1 5 10 <210> 3014 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3014 Val Ser Pro Gly Gln Thr Ala Ser Ile Thr 1 5 10 <210> 3015 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3015 Ala Ala Pro Gly Gln Lys Val Thr Ile Ser 1 5 10 <210> 3016 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3016 Ala Ala Pro Gly Gln Lys Val Thr Ile Ser 1 5 10 <210> 3017 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3017 Glu Ala Pro Arg Gln Arg Val Thr Ile Ser 1 5 10 <210> 3018 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3018 Glu Ala Pro Arg Gln Arg Val Thr Ile Ser 1 5 10 <210> 3019 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3019 Val Ser Pro Gly Gln Thr Ala Ser Ile Thr 1 5 10 <210> 3020 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3020 Ser Pro Gly Phe Pro Gly Glu Tyr Ala Asn 1 5 10 <210> 3021 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3021 Leu Ser Pro Gly Glu Arg Ala Thr Leu Ser 1 5 10 <210> 3022 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3022 Leu Ser Pro Gly Glu Arg Ala Thr Leu Ser 1 5 10 <210> 3023 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3023 Leu Gly Gln Pro Ala Ser Ile Ser Cys Arg 1 5 10 <210> 3024 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3024 Leu Pro Val Thr Leu Gly Gln Pro Ala Ser 1 5 10 <210> 3025 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3025 Arg Leu Arg Arg Gly Leu Pro Ala Leu Leu 1 5 10 <210> 3026 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3026 Arg Arg Gly Leu Pro Ala Leu Leu Arg Ala 1 5 10 <210> 3027 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3027 Gln Ala Glu Ala Lys Ser Tyr Phe Glu Lys 1 5 10 <210> 3028 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3028 Leu Gly Gln Pro Ala Ser Ile Ser Phe Arg 1 5 10 <210> 3029 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3029 Ser Pro Val Thr Leu Gly Gln Pro Ala Ser 1 5 10 <210> 3030 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3030 Thr Phe Gly Ser Gly Glu Ala Asp Cys Gly 1 5 10 <210> 3031 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3031 Thr Phe Gly Ser Gly Glu Ala Asp Cys Gly 1 5 10 <210> 3032 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3032 Arg Arg Ala Asn Thr Phe Leu Glu Glu Val 1 5 10 <210> 3033 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3033 Arg Tyr Asn Ser Gly Lys Leu Glu Glu Phe 1 5 10 <210> 3034 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3034 Arg Tyr Asn Ser Gly Lys Leu Glu Glu Phe 1 5 10 <210> 3035 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3035 Asp Trp Ala Ala Gly Thr Met Asp Pro Glu 1 5 10 <210> 3036 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3036 Leu Gly Asp Trp Ala Ala Gly Thr Met Asp 1 5 10 <210> 3037 <211> 29 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3037 Asp Val Gly Ser Tyr Gln Glu Lys Val Asp Val Val Leu Gly Pro Ile 1 5 10 15 Gln Leu Gln Thr Pro Pro Arg Arg Glu Glu Glu Pro Arg 20 25 <210> 3038 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3038 Lys Arg Glu Trp Val Lys Phe Ala Lys Pro 1 5 10 <210> 3039 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3039 Lys Arg Glu Trp Val Lys Phe Ala Lys Pro 1 5 10 <210> 3040 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3040 Ala Val Val Pro Ser Thr Ala Thr Val Val 1 5 10 <210> 3041 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3041 Ala Val Val Pro Ser Thr Ala Thr Val Val 1 5 10 <210> 3042 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3042 Thr Thr Thr Pro Ser Lys Gln Ser Asn Asn 1 5 10 <210> 3043 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3043 Leu Thr Pro Glu Gln Trp Lys Ser His Lys 1 5 10 <210> 3044 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3044 Leu Thr Pro Glu Gln Trp Lys Ser His Lys 1 5 10 <210> 3045 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3045 Ala Ser Glu Asn Ile Val Ile Gln Val Tyr 1 5 10 <210> 3046 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3046 Ala Ala Pro Gln Ser Val Cys Ala Leu Arg 1 5 10 <210> 3047 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3047 Thr Glu Thr Thr Glu Lys Gly Cys Val Leu 1 5 10 <210> 3048 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3048 Ile Asn Asn Pro Leu Ala Gln Ala Asp Trp 1 5 10 <210> 3049 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3049 Ile Phe Ala Gly Leu Ala Phe Ile Val Gly 1 5 10 <210> 3050 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3050 Phe Tyr Tyr Asp Tyr Glu Thr Val Arg Asn 1 5 10 <210> 3051 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3051 Leu Pro Val Thr Pro Gly Glu Pro Ala Ser 1 5 10 <210> 3052 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3052 Pro Gly Glu Pro Ala Ser Ile Ser Cys Arg 1 5 10 <210> 3053 <211> 26 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3053 Gly Ala Gly Gly Glu Asp Ser Ala Gly Leu Gln Gly Gln Thr Leu Thr 1 5 10 15 Gly Gly Pro Ile Arg Ile Asp Trp Glu Asp 20 25 <210> 3054 <211> 29 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3054 His Asp Asn Leu Arg Ser Leu Asp Arg Asn Leu Pro Ser Asp Ser Gln 1 5 10 15 Asp Leu Gly Gln His Gly Leu Glu Glu Asp Phe Met Leu 20 25 <210> 3055 <211> 21 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3055 Lys Pro Gly Val Tyr Thr Asp Val Ala Tyr Tyr Leu Ala Trp Ile Arg 1 5 10 15 Glu His Thr Val Ser 20 <210> 3056 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3056 Gly Val Asn Leu Gln Glu Phe Leu Asn Val 1 5 10 <210> 3057 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3057 Lys Arg Gly Ile Val Glu Gln Cys Cys Thr 1 5 10 <210> 3058 <211> 16 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3058 Ser Gly Phe Pro Gln Val Ser Met Phe Phe Thr His Thr Phe Pro Lys 1 5 10 15 <210> 3059 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3059 Leu Ser Pro Gly Glu Arg Ala Thr Leu Ser 1 5 10 <210> 3060 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3060 Ala Ser Val Gly Asp Arg Val Thr Ile Thr 1 5 10 <210> 3061 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3061 Glu Lys Ala His Asp Gly Gly Arg Tyr Tyr 1 5 10 <210> 3062 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3062 Gln Val Arg Leu Leu Gln Arg Leu Lys Thr 1 5 10 <210> 3063 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3063 Tyr Ser Leu Phe Arg Glu Gln Asp Ala Pro 1 5 10 <210> 3064 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3064 Ser Tyr Pro Ala Ala Ala Ala Ala Lys Val 1 5 10 <210> 3065 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3065 Leu Gln Asp Pro Val Leu Val Ser Cys Asp 1 5 10 <210> 3066 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3066 Lys Arg Arg Asp Phe Thr Pro Ala Glu Leu 1 5 10 <210> 3067 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3067 Glu Ser Pro Gly Lys Thr Val Thr Ile Ser 1 5 10 <210> 3068 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3068 Glu Ser Pro Gly Lys Thr Val Thr Ile Ser 1 5 10 <210> 3069 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3069 Val Ser Pro Gly Glu Arg Ala Thr Leu Ser 1 5 10 <210> 3070 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3070 Ser Pro Gly Tyr Pro Glu Pro Tyr Gly Lys 1 5 10 <210> 3071 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3071 Lys Lys Ala Gly Gly Thr Pro Arg Lys Ala 1 5 10 <210> 3072 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3072 Lys Pro Pro Pro Gln Lys Ser Leu Lys Glu 1 5 10 <210> 3073 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3073 Arg Arg Ser Phe Pro Glu Pro Glu Glu Pro 1 5 10 <210> 3074 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3074 Tyr Val His Leu Arg Pro Ala Arg Pro Thr 1 5 10 <210> 3075 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3075 Gly Ser Pro Gly Gln Ser Val Thr Ile Ser 1 5 10 <210> 3076 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3076 Gly Ser Pro Gly Gln Ser Val Thr Ile Ser 1 5 10 <210> 3077 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3077 Gln Pro Leu Val Val Pro Trp Glu Ala Ser 1 5 10 <210> 3078 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3078 Ser Met Pro Pro Ala Gln Gln Gln Ile Thr 1 5 10 <210> 3079 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3079 Arg Ala Asp Glu Pro Gln Trp Ser Leu Tyr 1 5 10 <210> 3080 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3080 Ala Ala Asp Ile Pro Glu Val Val Val Ser 1 5 10 <210> 3081 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3081 Lys Pro Glu His Phe Leu Asn Glu Asn Gly 1 5 10 <210> 3082 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3082 Tyr Ala Glu Gly Thr Phe Ile Ser Asp Tyr 1 5 10 <210> 3083 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3083 Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe 1 5 10 <210> 3084 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3084 Gly Ser Pro Gly Gln Ser Val Thr Ile Ser 1 5 10 <210> 3085 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3085 Pro Gly Pro Met Lys Lys Asp Lys Asp Gln 1 5 10 <210> 3086 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3086 Lys Val Ser Val Asp Glu Pro Gly Pro Gly 1 5 10 <210> 3087 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3087 Arg Ser Ser Arg Ile Gly Glu Ile Lys Glu 1 5 10 <210> 3088 <211> 4 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3088 Leu Ile Cys Ser One <210> 3089 <211> 37 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3089 Leu Thr Phe Pro Leu Asp Tyr His Leu Asn Gln Pro Phe Ile Phe Val 1 5 10 15 Leu Arg Asp Thr Asp Thr Gly Ala Leu Leu Phe Ile Gly Lys Ile Leu 20 25 30 Asp Pro Arg Gly Pro 35 <210> 3090 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3090 Lys Glu Leu Arg Asn His Gln Pro Arg Glu 1 5 10 <210> 3091 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3091 Val Ser Pro Gly Gln Thr Ala Arg Ile Thr 1 5 10 <210> 3092 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3092 Asn Pro Val Tyr His Leu Asn Asn Pro Ile 1 5 10 <210> 3093 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3093 Ala Thr Leu Ser Val His Gln Leu Val Glu 1 5 10 <210> 3094 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3094 Lys Arg Asp Thr Gly Ala Ala Leu Leu Ala 1 5 10 <210> 3095 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3095 Ser Leu Gly Glu Arg Ala Thr Ile Asn Cys 1 5 10 <210> 3096 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3096 Ser Pro Leu Phe Pro Lys Pro Tyr Pro Asn 1 5 10 <210> 3097 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3097 Ala Ala Ser Ala Val Pro Ala Ser Gly Val 1 5 10 <210> 3098 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3098 Val Asp Ala Lys Ala Gln Val Lys Thr Glu 1 5 10 <210> 3099 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3099 Ala Ala Pro Pro Ala Ala Ala Thr Ile Ser 1 5 10 <210> 3100 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3100 Val Pro Lys Asp Leu Pro Pro Asp Thr Thr 1 5 10 <210> 3101 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3101 Leu Leu Ala Arg Asp Phe Glu Lys Asn Tyr 1 5 10 <210> 3102 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3102 Ile Lys Ala Pro Lys Leu Pro Gly Gly Tyr 1 5 10 <210> 3103 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3103 Gly Val Pro Gly Ala Gly Val Pro Gly Val 1 5 10 <210> 3104 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3104 Leu Thr Gly Pro Ile Gly Pro Pro Gly Pro 1 5 10 <210> 3105 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3105 Pro Gly Leu Lys Gly Lys Arg Gly Asp Ser 1 5 10 <210> 3106 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3106 Ile Ser Gln Asp Leu Glu Lys Gln Ala Ala 1 5 10 <210> 3107 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3107 Leu Leu Gln Asp Ser Val Asp Phe Ser Leu 1 5 10 <210> 3108 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3108 Gly Leu Pro Gly Thr Gly Gly Pro Pro Gly 1 5 10 <210> 3109 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3109 Ile Leu Gly His Val Pro Gly Met Leu Leu 1 5 10 <210> 3110 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3110 Pro Gly Asp Ile Val Phe Arg Lys Gly Pro 1 5 10 <210> 3111 <211> 11 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3111 Asp Thr Gly Pro Gly Ala Arg Glu Lys Gly Glu 1 5 10 <210> 3112 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3112 Gly Pro Arg Val Val Glu Arg His Gln Ser 1 5 10 <210> 3113 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3113 Gly Pro Arg Val Val Glu Arg His Gln Ser 1 5 10 <210> 3114 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3114 Gln Ala Ala Ala Ala Ala Lys Ala Ala Lys 1 5 10 <210> 3115 <211> 6 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3115 Lys Ala Phe Val Phe Pro 1 5 <210> 3116 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3116 Val Ala Ala Ala Ala Lys Ser Ala Ala Lys 1 5 10 <210> 3117 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3117 Tyr Arg Gly Pro Glu Gly Pro Gln Gly Pro 1 5 10 <210> 3118 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3118 His Met Gly Arg Glu Gly Arg Glu Gly Glu 1 5 10 <210> 3119 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3119 Gly Leu Glu Glu Glu Leu Gln Phe Ser Leu 1 5 10 <210> 3120 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3120 Ser Glu Glu Thr Lys Glu Asn Glu Gly Phe 1 5 10 <210> 3121 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3121 Asp Cys Asp Asp Val Leu Gln Thr His Pro 1 5 10 <210> 3122 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3122 His Ile Leu Gly Ala Ala Gly Ala Thr Asp 1 5 10 <210> 3123 <211> 10 <212> PRT <213> artificial sequence <220> <223> synthetic <400> 3123 Pro Arg Gly Glu Thr Gly Asp Asp Gly Arg 1 5 10 <210> 3124 <211> 23 <212> PRT <213> artificial sequence <220> <223> Collagen I Cleaveage Site <400> 3124 Gly Ala Asp Gly Ser Pro Gly Lys Asp Gly Val Arg Gly Leu Thr Gly 1 5 10 15 Pro Ile Gly Pro Pro Gly Pro 20 <210> 3125 <211> 26 <212> PRT <213> artificial sequence <220> <223> 818-Non Clv <400> 3125 Ala Pro Thr Thr Gly Glu Ala Gly Glu Ala Ala Gly Ala Thr Ser Ala 1 5 10 15 Gly Ala Thr Gly Pro Ala Thr Ser Gly Ser 20 25 <210> 3126 <211> 26 <212> PRT <213> artificial sequence <220> <223> AMX-818 Cleave Site <400> 3126 Gly Gly Ser Ala Pro Glu Ala Gly Arg Ser Ala Asn His Thr Pro Ala 1 5 10 15 Gly Leu Thr Gly Pro Ala Thr Ser Gly Ser 20 25 <210> 3127 <211> 26 <212> PRT <213> artificial sequence <220> <223> AC2566 Cleavage Site <400> 3127 Gly Gly Ser Ala Pro Glu Ala Gly Arg Ser Ala Asn His Gly Val Arg 1 5 10 15 Gly Leu Thr Gly Pro Ala Thr Ser Gly Ser 20 25 <210> 3128 <211> 26 <212> PRT <213> artificial sequence <220> <223> AC2567 Cleavage Site <400> 3128 Gly Gly Ser Ala Pro Glu Ala Gly Ser Pro Gly Lys Asp Gly Val Arg 1 5 10 15 Gly Leu Thr Gly Pro Ala Thr Ser Gly Ser 20 25 <210> 3129 <211> 23 <212> PRT <213> artificial sequence <220> <223> E. coli AmE098 <400> 3129 Met Lys Lys Asn Ile Ala Phe Leu Leu Ala Ser Met Phe Val Phe Ser 1 5 10 15 Ile Ala Thr Asn Ala Tyr Ala 20

Claims (106)

A method for assessing the likelihood that a subject suffering from a disease or disorder will respond to a therapeutic agent that can be activated by a mammalian protease expressed in the subject,
a. determining the presence or amount of a proteolytic peptide product produced by the action of said mammalian protease in a biological sample from said subject affected by a disease or disorder, wherein said peptide is
i. comprises at least 5 or 6 contiguous amino acid residues indicated in the sequence set forth in column V of Table A ;
ii. contains at least 5 or 6 contiguous amino acids indicated in the sequence set forth in column IV of Table A ;
iii. comprising at least 5 or 6 contiguous amino acids indicated in the sequence set forth in column VI of Table A ; and
b. designating said subject as likely to respond to said therapeutic agent if said peptide of (i), (ii) or (iii) is present and/or if its amount exceeds a threshold value. The method of claim 1 , wherein the therapeutic agent comprises a peptide substrate having an amino acid sequence susceptible to cleavage by the mammalian protease at its cleavable linkage. 3. The method of claim 2, wherein said polypeptide of (i), (ii) or (iii) is at least 4, at least 5, at least 4, at least 5, at least of said sequence of said peptide substrate which is on the N-terminal or C-terminal side of said scissile bond. A method comprising a portion comprising 6, at least 7, at least 8, at least 9 or at least 10 contiguous amino acid residues. 3. The method according to claim 1 or 2, wherein said sequence of the peptide substrate is susceptible to cleavage by said mammalian protease at a scissile bond, wherein said polypeptide of (i), (ii) or (iii) is not subject to cleavage. is a cleavage product of a reporter polypeptide comprising a substrate sequence that is susceptible to cleavage by the same mammalian protease at easy linkage, wherein the reporter polypeptide comprises the sequence set forth in column II or column III of Table A. 3. The method according to claim 1 or 2, wherein said sequence of the peptide substrate is susceptible to cleavage by said mammalian protease at a scissile bond, wherein said polypeptide of (i), (ii) or (iii) is not subject to cleavage. A cleavage product of a human protein comprising a portion comprising at least 5 or 6 contiguous amino acid residues of said peptide substrate sequence comprising easy linkage. 6 . The polypeptide of claim 1 , wherein the polypeptide of (i) comprises at least 7, at least 8, at least 9 or at least 10 contiguous amino acid residues represented in the sequence set forth in column V of Table A. Including, how. 7. The method according to any one of claims 1 to 6, wherein said polypeptide of (ii) comprises at least 7, at least 8, at least 9 or at least 10 contiguous amino acids indicated in the sequence set forth in column IV of Table A. How to do it. 8. The method of any one of claims 1 to 7, wherein said polypeptide of (iii) comprises at least 7, at least 8, at least 9 or at least 10 contiguous amino acids indicated in the sequence set forth in column VI of Table A. How to do it. 9. The method of any preceding claim, wherein step (a) comprises determining the presence or amount of any two of (i) to (iii). 10. A method according to any one of claims 1 to 9, wherein the threshold is zero or a nominal threshold. 11. The method of any one of claims 1 to 10, wherein the biological sample comprises a serum or plasma sample. 12. The method according to any one of claims 1 to 11, wherein the mammalian protease is a serine protease, a cysteine protease, an aspartate protease, a threonine protease or a metalloproteinase. The method of claim 12, wherein the mammalian protease is disintegrin and metalloproteinase domain-containing protein 10 (ADAM10), disintegrin and metalloproteinase domain-containing protein 12 (ADAM12), disintegrin and metalloproteina protein 15 (ADAM15) containing the first domain, protein 17 (ADAM17) containing disintegrin and metalloproteinase domains, protein 9 (ADAM9) containing disintegrin and metalloproteinase domains, disintegrin with thrombospondin motif 5 and metalloproteinase (ADAMTS5), cathepsin B, cathepsin D, cathepsin E, cathepsin K, cathepsin L, cathepsin S, fibroblast activation protein alpha, hepsin, kallikrein-2, kallikrein- 4, kallikrein-3, prostate specific antigen (PSA), kallikrein-13, legumain, matrix metallopeptidase 1 (MMP-1), matrix metallopeptidase 10 (MMP-10), Matrix Metallopeptidase 11 (MMP-11), Matrix Metallopeptidase 12 (MMP-12), Matrix Metallopeptidase 13 (MMP-13), Matrix Metallopeptidase 14 (MMP-14) ), matrix metallopeptidase 16 (MMP-16), matrix metallopeptidase 2 (MMP-2), matrix metallopeptidase 3 (MMP-3), matrix metallopeptidase 7 (MMP -7), matrix metallopeptidase 8 (MMP-8), matrix metallopeptidase 9 (MMP-9), matrix metallopeptidase 4 (MMP-4), matrix metallopeptidase 5 (MMP-5), matrix metallopeptidase 6 (MMP-6), matrix metallopeptidase 15 (MMP-15), neutrophil elastase, protease activated receptor 2 (PAR2), plasmin, prostar Shin, PSMA-FOLH1, membrane type serine protease 1 (MT-SP1), matriptase and u-plasminogen are selected from the group consisting of. 13. The method of claim 12, wherein the mammalian protease is matrix metallopeptidase 1 (MMP1), matrix metallopeptidase 2 (MMP2), matrix metallopeptidase 7 (MMP7), matrix metallopeptidase 9 (MMP9), matrix metallopeptidase 11 (MMP11), matrix metallopeptidase 14 (MMP14), urokinase-type plasminogen activator (uPA), legumain and matriptase How to be. 15. The method of any one of claims 1 to 14, wherein the mammalian protease is preferentially expressed or activated in a target tissue or cell. 16. The method of claim 15, wherein the target tissue or cell is a tumor. 17. The method of claim 15 or 16, wherein the target tissue or cell produces or colocalizes with the mammalian protease. 18. The method of any one of claims 15 to 17, wherein the target tissue or cell contains a reporter polypeptide in or on it or is associated with the reporter polypeptide in proximity thereto. 19. The method of claim 4 or 18, wherein the reporter polypeptide is a coagulation factor, complement component, tubulin, immunoglobulin, apolipoprotein, serum amyloid, insulin, growth factor, fibrinogen, PDZ domain protein, LIM domain protein, c- Reactive protein, serum albumin, versican, collagen, elastin, keratin, kininogen-1, alpha-2-antiplasmin, clusterin, biglycan, alpha-1-antitrypsin, transthyretin, alpha- 1-antichymotrypsin, glucagon, hepcidin, thymosin beta-4, haptoglobin, hemoglobin subunit alpha, vesicle-associated protein 2, alpha-2-HS-glycoprotein, chromogranin-A, vitronectin, Hemopexin, epididymal secreted sperm binding protein, secretogranin-2, angiotensinogen, transgelin-2, pancreatic prohormone, neurosecretory protein VGF, ceruloplasmin, PDZ and LIM domain protein 1, multimerin- 1, inter-alpha-trypsin inhibitor heavy chain H2, N-acetylmuramoyl-L-alanine amidase, histone H1.4, adhesion G-protein coupled receptor G6, mannan binding lectin serine protease 2, prothrombin, deleted in malignant brain tumor deleted in malignant brain tumors 1 protein, desmoglein-3, calcintenin-1, alpha-2-macroglobulin, myosin-9, sodium/potassium transport ATPase subunit gamma, oncoprotein-derived transcript 3 proteins, serglycine, histidine rich glycoprotein, inter-alpha-trypsin inhibitor heavy chain H5, integrin alpha-IIb, membrane associated progesterone receptor component 1, histone H1.2, rho GDP-dissociation inhibitor 2, zinc-alpha -2-Glycoprotein, Talin-1, Secretogranin-1, Neutrophil Defensin 3, Cytochrome P450 2E1, Gastric Inhibitory Polypeptide, Transcription Initiation Factor TFIID Subunit 1, Integral Membrane Protein 2B, Pigment Epithelial Derived Factor, Voltage Dependent N-type calcium channel subunit alpha-1B, ras GTPase-activating protein nGAP, type I cytoskeleton 17, sulfhydryl oxidase 1, homeobox protein Hox-B2, transcription factor SOX-10, E3 ubiquitin-protein ligase A polypeptide selected from the group consisting of SIAH2, decorin, secreted protein acidic and rich in cysteine (SPARC), laminin gamma 1 chain, vimentin and nidogen-1 (NID1). 19. The method of claim 4 or 18, wherein the reporter polypeptide is versican, type II collagen alpha-1 chain, kininogen-1, complement C4-A, complement C4-B, complement C3, alpha-2-antigen Plasmin, clustererin, biglycan, elastin, fibrinogen alpha chain, alpha-1-antitrypsin, fibrinogen beta chain, type III collagen alpha-1 chain, serum amyloid A-1 protein, transthyretin, apolipoprotein A-I , apolipoprotein A-I isoform 1, alpha-1-antichymotrypsin, glucagon, hepcidin, serum amyloid A-2 protein, thymosin beta-4, haptoglobin, hemoglobin subunit alpha, vesicle-associated protein 2, alpha -2-HS-glycoprotein, chromogranin-A, vitronectin, hemopexin, epididymal secreted sperm binding protein, direct skin, apolipoprotein C-III, secretogranin-2, angiotensinogen, c- Reactive protein, serum albumin, transgelin-2, pancreatic prohormone, neurocrine protein VGF, ceruloplasmin, PDZ and LIM domain protein 1, tubulin alpha-4A chain, multimerin-1, inter-alpha-trypsin inhibitor Heavy chain H2, apolipoprotein C-I, fibrinogen gamma chain, N-acetylmuramoyl-L-alanine amidase, immunoglobulin lambda variable 3-21, histone H1.4, attached G-protein coupled receptor G6, immunoglobulin lambda variable 3 -25, immunoglobulin lambda variable 1-51, immunoglobulin lambda variable 1-36, mannan-binding lectin serine protease 2, immunoglobulin kappa variable 3-20, immunoglobulin kappa variable 2-30, insulin-like growth factor II, apolilipid Protein A-II, probable nonfunctional immunoglobulin kappa variable 2D-24, prothrombin, coagulation factor IX, apolipoprotein L1, protein 1 deleted in malignant brain tumor, desmoglein-3, calcintenin-1, immunoglobulin lambda constant 3, complement C5, alpha-2-macroglobulin, myosin-9, sodium/potassium transport ATPase subunit gamma, immunoglobulin kappa variable 2-28, oncoprotein derived transcript 3 protein, serglycin, coagulation factor XII, Coagulation factor XIII A chain, insulin, histidine rich glycoprotein, immunoglobulin kappa variable 3-11, immunoglobulin kappa variable 1-39, collagen alpha-1(I) chain, inter-alpha-trypsin inhibitor heavy chain H5, potential transforming growth factor beta binding protein 2, integrin alpha-IIb, membrane associated progesterone receptor component 1, immunoglobulin lambda variable 6-57, immunoglobulin kappa variable 3-15, complement C1r subcomponent-like protein, histone H1.2, rho GDP-dissociated inhibitor 2, potential transforming growth factor beta binding protein 4, collagen alpha-1 (XVIII) chain, immunoglobulin lambda variable 2-18, zinc-alpha-2-glycoprotein, talin-1, secretogranin-1, neutrophil defensin 3, cytochrome P450 2E1, gastric inhibitory polypeptide, immunoglobulin heavy chain variable 3-15, immunoglobulin lambda variable 2-11, transcription initiation factor TFIID subunit 1, collagen alpha-1 (VII) chain, integral membrane protein 2B, pigment epithelial-derived factor, voltage-dependent N-type calcium channel subunit alpha-1B, immunoglobulin lambda variable 3-27, ras GTPase-activating protein nGAP, keratin, type I cytoskeleton 17, tubulin beta chain, sulfhydryl oxidase 1, immunoglobulin kappa variable 4-1, complement C1r subcomponent, homeobox protein Hox-B2, transcription factor SOX-10, E3 ubiquitin-protein ligase SIAH2, decorin, SPARC, type I collagen alpha-1 chain, type IV collagen alpha-1 chain, laminin gamma 1 chain, vimentin, type III collagen, type IV collagen alpha-3 chain, type VII collagen alpha-1 chain, type VI collagen alpha-1 chain, type V collagen alpha-1 chain, a polypeptide selected from the group consisting of nidogen-1 and type VI collagen alpha-3 chains. 21. The method of any one of claims 18-20, wherein the reporter polypeptide comprises a sequence set forth in columns II-VI of Table A. 19. The method of any one of claims 15 to 18, wherein the target tissue or cell is characterized by an increased amount or activity of the mammalian protease proximal to the target tissue or cell compared to a non-target tissue or cell of the subject. How to do it. 23. The method of any one of claims 1 to 22, wherein the subject is characterized by increased expression or activity of the mammalian protease proximal to the target tissue or cell compared to the corresponding non-target tissue or cell of the subject. Suffering from or suspected of suffering from a disease or condition. 24. The method of claim 23, wherein the disease or condition is cancer or an inflammatory or autoimmune disease. 25. The method of claim 24, wherein the disease or condition is carcinoma, Hodgkin's lymphoma and non-Hodgkin's lymphoma, diffuse large B cell lymphoma, follicular lymphoma, mantle cell lymphoma, blastoma, breast cancer, ER/PR+ breast cancer, Her2+ breast cancer, triple negative breast cancer. , colorectal cancer, colorectal cancer with malignant ascites, mucinous tumor, prostate cancer, head and neck cancer, skin cancer, melanoma, genitourinary cancer, ovarian cancer, ovarian cancer with malignant ascites, peritoneal carcinomatosis, uterine serous carcinoma, Endometrial cancer, cervical cancer, colorectal cancer, uterine cancer, peritoneal mesothelioma, kidney cancer, Wilms' tumor, lung cancer, small cell lung cancer, non-small cell lung cancer, gastric cancer, stomach cancer, small intestine cancer, liver cancer, hepatocarcinoma, hepatoblastoma , Liposarcoma, pancreatic cancer, gallbladder cancer, cholangiocarcinoma, esophageal cancer, salivary gland carcinoma, thyroid cancer, epithelial cancer, androgenic germ cell tumor, adenocarcinoma, sarcoma, and B-cell derived chronic lymphocytic leukemia. 25. The method of claim 24, wherein the disease or condition is ankylosing spondylitis (AS), arthritis (eg, rheumatoid arthritis (RA), juvenile idiopathic arthritis (JIA), osteoarthritis (OA), psoriatic arthritis (PsA), gout, chronic arthritis, but not limited to), Chagas disease, chronic obstructive pulmonary disease (COPD), dermatomyositis, type 1 diabetes, endometriosis, Goodpasture syndrome, Graves disease, Guillain-Barré syndrome (GBS), Hashimoto disease , purulent scab, Kawasaki disease, IgA nephropathy, idiopathic thrombocytopenic purpura, inflammatory bowel disease (IBD) (eg, Crohn's disease (CD), clonal disease, ulcerative colitis, collagenous colitis, lymphocytic colitis, ischemic colitis, empty colitis, Behcet's syndrome, infectious colitis, indeterminate colitis, interstitial cystitis, but not limited to), lupus (eg, systemic lupus erythematosus, discoid lupus, subacute cutaneous lupus erythematosus, cutaneous erythematosus lupus (e.g., alumni lupus erythematosus), drug-induced lupus, neonatal lupus, lupus nephritis, but not limited to, mixed connective tissue disease, focal dermatosclerosis, multiple sclerosis (MS), severe muscle weakness, narcolepsy, neuromuscular Angina pectoris, pemphigus vulgaris, pernicious anemia, psoriasis, psoriatic arthritis, polymyositis, primary biliary cirrhosis, recurrent polychondritis, schizophrenia, scleroderma, Sjogren's syndrome, systemic stiffness syndrome, temporal arteritis (also called giant cell arteritis) , vasculitis, vitiligo, Wegener's granulomatosis, immune response associated with transplant rejection (eg, but not limited to, kidney transplant rejection, lung transplant rejection, liver transplant rejection), psoriasis, Wiskott-Aldrich syndrome, autoimmune lymphoproliferative syndrome, myasthenia gravis, chronic inflammatory rhinosinusitis, colitis, chronic digestive disorder, Barrett's esophagus, inflammatory gastritis, autoimmune nephritis, autoimmune hepatitis, autoimmune carditis, autoimmune encephalitis, autoimmune mediated blood disorders, asthma, atopy It is selected from the group consisting of dermatitis, atopy, allergy, allergic rhinitis, scleroderma, bronchitis, and pericarditis, and the inflammatory disease is Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis, inflammatory lung disease, inflammatory skin disease, atherosclerosis, myocardial infarction, stroke, gram-positive shock, gram-negative shock, sepsis, septic shock, hemorrhagic shock, anaphylactic shock, systemic inflammatory response syndrome. 27. The method of any one of claims 1-26, wherein the therapeutic agent is an anti-cancer agent. 28. The method of any one of claims 1-27, wherein the therapeutic agent is an activatable therapeutic agent. 29. The method of any one of claims 1-28, wherein the therapeutic agent further comprises a masking moiety (MM). 30. The method of claim 29, wherein the masking moiety (MM) is capable of being released from the therapeutic upon cleavage of the peptide substrate by the mammalian protease. 31. The method of claim 29 or 30, wherein the masking moiety (MM), in its uncleaved state, interferes with the interaction of the therapeutic agent to a target tissue or cell. 32. The method of any one of claims 29-31, wherein the bioactivity of the therapeutic agent can be improved upon cleavage of the peptide substrate by the mammalian protease. 33. The method of any one of claims 29-32, wherein the masking moiety (MM) is an extended recombinant polypeptide (XTEN). 34. The method of claim 33, wherein the XTEN is
(i) contains at least 100 amino acids;
(ii) at least 90% of the amino acid residues are selected from glycine (G), alanine (A), serine (S), threonine (T), glutamate (E) and proline (P);
(iii) at least four different types of amino acids selected from G, A, S, T, E and P. 35. The method of any one of claims 1-34, further comprising the step (b) thereafter contacting the therapeutic agent with the mammalian protease to assess whether the subject will respond to the therapeutic agent. 35. The method of any one of claims 1-34, wherein (a) comprises detecting the polypeptide of (i), (ii) or (iii) in an immunoassay. 37. The method of claim 36, wherein the immunoassay uses an antibody that specifically binds to the polypeptide of (i), (ii) or (iii) or an epitope thereof. 38. The method of any one of claims 1-37, wherein (a) comprises detecting the polypeptide of (i), (ii) or (iii) using mass spectrometry (MS). method. 39. The method of any one of claims 1-38, further comprising, after (b), administering to the subject an effective amount of the therapeutic agent based on the specifications in step (b). A method of treating a subject with an activatable therapeutic agent, comprising:
(a) identifying the subject as likely to respond to the activatable therapeutic agent based on identification of a peptide biomarker in a biological sample from the subject, wherein the activatable therapeutic agent binds to a mammalian protease at a cleavable bond. comprising a peptide substrate sequence susceptible to cleavage by; and
(b) administering the activatable therapeutic agent to the subject based on the identification of the subject in (a);
wherein the peptide biomarker comprises a portion identical to at least four consecutive amino acid residues of the peptide substrate sequence that is the N-terminus or C-terminus of the cleavable bond. 41. The method of claim 40, wherein the peptide biomarker is derived from a reporter polypeptide, wherein the reporter polypeptide comprises the sequence set forth in columns II - VI of Table A. 42. The method of claim 40 or 41, wherein the peptide biomarker has an amino acid sequence identical to that of the reporter polypeptide, and wherein the reporter polypeptide comprises the sequence set forth in columns II - VI of Table A. 43. The method of any one of claims 40-42, wherein the peptide substrate sequence contains 6 to 25 or 6 to 20 amino acid residues. 44. The method of claim 43, wherein the peptide substrate sequence contains 7 to 12 amino acid residues. 45. The method of any one of claims 40 to 44, wherein the peptide substrate sequence has up to 3 amino acid substitutions, up to 2 amino acid substitutions, or up to 1 amino acid substitution relative to the sequence set forth in column II or column III of Table A. wherein none of the amino acid substitutions is at a position corresponding to an amino acid residue immediately adjacent to the corresponding scissile bond as shown in Table A. 46. The method of claim 45, wherein the peptide substrate sequence comprises the amino acid sequence set forth in column II or column III of Table A. 47. The method of any one of claims 40-46, wherein the peptide substrate sequence susceptible to cleavage by the mammalian protease is susceptible to cleavage by a plurality of mammalian proteases, including the mammalian protease. 48. The method of claim 47, wherein said peptide substrate sequence susceptible to cleavage by said plurality of mammalian proteases has at most three amino acid substitutions, at most two amino acid substitutions, or at most one amino acid substitution relative to the sequence set forth in Table 1(j). wherein none of the amino acid substitutions is at a position corresponding to an amino acid residue immediately adjacent to the corresponding scissile bond. 49. The method of claim 47 or 48, wherein the peptide substrate sequence susceptible to cleavage by the plurality of mammalian proteases comprises a sequence set forth in Table 1(j) . 46. The method of claim 45, wherein the peptide substrate sequence has the same amino acid sequence as a fragment of the sequence set forth in column II or III of Table A , wherein the fragment is at least immediately adjacent to the corresponding scissile bond as shown in Table A. A method comprising four consecutive amino acid residues. 51. The method of claim 50, wherein the fragment contains at least 5, at least 6, at least 7, at least 8, at least 9 or at least 10 amino acid residues. 52. The portion of the peptide substrate sequence according to any one of claims 40 to 51 that is the N-terminus of the scissile bond is between 4 and 10 amino acid residues of the sequence set forth in column IV or column V of Table A. with up to 3 amino acid substitutions, up to 2 amino acid substitutions, or up to 1 amino acid substitution, with respect to the sequence of the C-terminal end containing, wherein any of the amino acid substitutions is at the amino acid residue immediately adjacent to the corresponding scissile bond which is not in the corresponding position. 53. The C-terminal end of claim 52, wherein said portion of said peptide substrate sequence that is N-terminal of said scissile bond contains 4 to 10 amino acid residues of the sequence set forth in column IV or column V of Table A. The method comprising the sequence of. 53. The portion of the peptide substrate sequence according to any one of claims 40 to 52 that is the C-terminus of the scissile bond is between 4 and 10 amino acid residues of the sequence set forth in column V or column VI of Table A. with up to 3 amino acid substitutions, up to 2 amino acid substitutions, or up to 1 amino acid substitution, with respect to the sequence of the N-terminal end containing, wherein any of the amino acid substitutions is at the amino acid residue immediately adjacent to the corresponding scissile bond which is not in the corresponding position. 55. The N-terminal end of claim 54, wherein said portion of said peptide substrate sequence that is C-terminal to said cleavable linkage contains 4 to 10 amino acid residues of the sequence set forth in column V or column VI of Table A. The method comprising the sequence of. 56. The method according to any one of claims 40 to 55, wherein said likelihood of said reaction is determined by the method according to any one of claims 1 to 39. A method of treating a subject in need of a therapeutic agent capable of being activated by a mammalian protease expressed in the subject, comprising:
Administering an effective amount of said therapeutic agent to said subject, wherein said subject has been shown to express in a biological sample from said subject:
(i) a polypeptide comprising at least 5 or 6 contiguous amino acid residues represented in the sequence set forth in column V of Table A ; or
(ii) a polypeptide comprising at least 5 or 6 contiguous amino acids as shown in the sequence set forth in column IV of Table A ; or
(iii) a polypeptide comprising at least 5 or 6 contiguous amino acids as shown in the sequence set forth in column VI of Table A ; or
(iv) the expression level of polypeptide (i), (ii) or (iii) exceeds a threshold value. 58. The method of claim 57, wherein the polypeptide sequence of (i) comprises at least 7, at least 8, at least 9 or at least 10 contiguous amino acid residues indicated in the sequence set forth in column V of Table A. 59. The method of claim 57 or 58, wherein the polypeptide of (ii) comprises at least 7, at least 8, at least 9 or at least 10 contiguous amino acids indicated in the sequence set forth in column IV of Table A , method. 60. The method of any one of claims 57-59, wherein said polypeptide of (iii) comprises at least 7, at least 8, at least 9 or at least 10 contiguous amino acids indicated in the sequence set forth in column VI of Table A. How to do it. 61. The method of any one of claims 57-60, wherein the subject has been shown to express any two of (i) to (iii) in the biological sample. 62. The method of any one of claims 57-61, wherein the therapeutic agent comprises a peptide substrate sequence susceptible to cleavage by the mammalian protease. 63. The method of claim 62, wherein the peptide substrate sequence is susceptible to cleavage by the mammalian protease at the cleavable linkage, wherein the polypeptide of (i), (ii) or (iii) is the N of the cleavable linkage. A method comprising a portion comprising at least 4 contiguous amino acid residues of a peptide substrate sequence that is -terminal or C-terminal. 64. The method of claim 63, wherein the portion of the peptide substrate sequence that is N-terminal of the cleavable bond is the C-terminal end of the sequence containing 4 to 10 amino acid residues of the sequence set forth in column IV or column V of Table A. has up to 3 amino acid substitutions, up to 2 amino acid substitutions, or up to 1 amino acid substitutions relative to the sequence, wherein none of the amino acid substitutions is at a position corresponding to an amino acid residue immediately adjacent to the corresponding cleavable linkage. , method. 65. The method of claim 63 or 64, wherein said portion of said peptide substrate sequence that is N-terminal of said scissile bond contains 4 to 10 amino acid residues of the sequence set forth in column IV or column V of Table A. Including the sequence of the C- terminal end, the method. 66. The portion of the peptide substrate sequence according to any one of claims 63 to 65 that is the C-terminus of the scissile bond is between 4 and 10 amino acid residues of the sequence set forth in column V or column VI of Table A. with up to 3 amino acid substitutions, up to 2 amino acid substitutions, or up to 1 amino acid substitution, with respect to the sequence of the N-terminal end containing, wherein any of the amino acid substitutions is at the amino acid residue immediately adjacent to the corresponding scissile bond which is not in the corresponding position. 67. The portion of the peptide substrate sequence according to any one of claims 63 to 66, which is the C-terminus of the scissile bond, is between 4 and 10 amino acids of the sequence set forth in column V or column VI of Table A. A method comprising a sequence of the N-terminal end containing residues. 68. The method of any one of claims 57 to 67, wherein the threshold is zero or a nominal threshold. 69. The method of any one of claims 40-68, wherein the biological sample comprises a serum or plasma sample. 70. The method of any one of claims 40-69, wherein the mammalian protease is a serine protease, a cysteine protease, an aspartate protease, a threonine protease or a metalloproteinase. 71. The method of claim 70, wherein the mammalian protease is disintegrin and metalloproteinase domain containing protein 10 (ADAM10), disintegrin and metalloproteinase domain containing protein 12 (ADAM12), disintegrin and metalloproteina protein 15 (ADAM15) containing the first domain, protein 17 (ADAM17) containing disintegrin and metalloproteinase domains, protein 9 (ADAM9) containing disintegrin and metalloproteinase domains, disintegrin with thrombospondin motif 5 and metalloproteinase (ADAMTS5), cathepsin B, cathepsin D, cathepsin E, cathepsin K, cathepsin L, cathepsin S, fibroblast activation protein alpha, hepsin, kallikrein-2, kallikrein- 4, kallikrein-3, prostate specific antigen (PSA), kallikrein-13, legumain, matrix metallopeptidase 1 (MMP-1), matrix metallopeptidase 10 (MMP-10), Matrix Metallopeptidase 11 (MMP-11), Matrix Metallopeptidase 12 (MMP-12), Matrix Metallopeptidase 13 (MMP-13), Matrix Metallopeptidase 14 (MMP-14) ), matrix metallopeptidase 16 (MMP-16), matrix metallopeptidase 2 (MMP-2), matrix metallopeptidase 3 (MMP-3), matrix metallopeptidase 7 (MMP -7), matrix metallopeptidase 8 (MMP-8), matrix metallopeptidase 9 (MMP-9), matrix metallopeptidase 4 (MMP-4), matrix metallopeptidase 5 (MMP-5), matrix metallopeptidase 6 (MMP-6), matrix metallopeptidase 15 (MMP-15), neutrophil elastase, protease activated receptor 2 (PAR2), plasmin, prostar Shin, PSMA-FOLH1, membrane type serine protease 1 (MT-SP1), matriptase and u-plasminogen are selected from the group consisting of. 71. The method of claim 70, wherein the mammalian protease is matrix metallopeptidase 1 (MMP1), matrix metallopeptidase 2 (MMP2), matrix metallopeptidase 7 (MMP7), matrix metallopeptidase 9 (MMP9), matrix metallopeptidase 11 (MMP11), matrix metallopeptidase 14 (MMP14), urokinase-type plasminogen activator (uPA), legumain and matriptase How to be. 72. The method of any one of claims 40 to 71, wherein the mammalian protease is preferentially expressed or activated in a target tissue or cell. 74. The method of claim 73, wherein the target tissue or cell is a tumor. 75. The method of claim 73 or 74, wherein the target tissue or cell produces or colocalizes with the mammalian protease. 76. The method of any one of claims 73-75, wherein the target tissue or cell contains a reporter polypeptide in or on it or is associated with the reporter polypeptide in proximity thereto. 77. The method of claim 76, wherein the reporter polypeptide is a coagulation factor, complement component, tubulin, immunoglobulin, apolipoprotein, serum amyloid, insulin, growth factor, fibrinogen, PDZ domain protein, LIM domain protein, c-reactive protein, serum Albumin, versican, collagen, elastin, keratin, kininogen-1, alpha-2-antiplasmin, clustererin, biglycan, alpha-1-antitrypsin, transthyretin, alpha-1-antichymo Trypsin, glucagon, hepcidin, thymosin beta-4, haptoglobin, hemoglobin subunit alpha, vesicle-associated protein 2, alpha-2-HS-glycoprotein, chromogranin-A, vitronectin, hemopexin, epididymis secretory sperm binding protein, secretogranin-2, angiotensinogen, transgelin-2, pancreatic prohormone, neurosecretory protein VGF, ceruloplasmin, PDZ and LIM domain protein 1, multimerin-1, inter- Alpha-trypsin inhibitor heavy chain H2, N-acetylmuramoyl-L-alanine amidase, histone H1.4, adhesion G-protein coupled receptor G6, mannan binding lectin serine protease 2, prothrombin, 1 protein deleted in malignant brain tumors ( deleted in malignant brain tumors 1 protein), desmoglein-3, calcintenin-1, alpha-2-macroglobulin, myosin-9, sodium/potassium transport ATPase subunit gamma, oncoprotein-derived transcript 3 protein, ser Glycine, histidine rich glycoprotein, inter-alpha-trypsin inhibitor heavy chain H5, integrin alpha-IIb, membrane associated progesterone receptor component 1, histone H1.2, rho GDP-dissociation inhibitor 2, zinc-alpha-2-sugar Protein, Talin-1, Secretogranin-1, Neutrophil Defensin 3, Cytochrome P450 2E1, Gastric Inhibitory Polypeptide, Transcription Initiation Factor TFIID Subunit 1, Integral Membrane Protein 2B, Pigmented Epithelial Derived Factor, Voltage-dependent Type N Calcium Channel Subunit alpha-1B, ras GTPase-activating protein nGAP, type I cytoskeleton 17, sulfhydryl oxidase 1, homeobox protein Hox-B2, transcription factor SOX-10, E3 ubiquitin-protein ligase SIAH2, decorin , a polypeptide selected from the group consisting of secreted protein acidic and rich in cysteine (SPARC), laminin gamma 1 chain, vimentin, and nidogen-1 (NID1). 78. The method of claim 77, wherein the reporter polypeptide is versican, type II collagen alpha-1 chain, kininogen-1, complement C4-A, complement C4-B, complement C3, alpha-2-antiplasmin, clu Sterin, biglycan, elastin, fibrinogen alpha chain, alpha-1-antitrypsin, fibrinogen beta chain, type III collagen alpha-1 chain, serum amyloid A-1 protein, transthyretin, apolipoprotein A-I, apolipoprotein A-I isoform 1, alpha-1-antichymotrypsin, glucagon, hepcidin, serum amyloid A-2 protein, thymosin beta-4, haptoglobin, hemoglobin subunit alpha, vesicle-associated protein 2, alpha-2-HS -Glycoprotein, chromogranin-A, vitronectin, hemopexin, epididymal secreted sperm binding protein, direct skin, apolipoprotein C-III, secretogranin-2, angiotensinogen, c-reactive protein, serum Albumin, transgelin-2, pancreatic prohormone, neurosecretory protein VGF, ceruloplasmin, PDZ and LIM domain protein 1, tubulin alpha-4A chain, multimerin-1, inter-alpha-trypsin inhibitor heavy chain H2, apo Lipoprotein C-I, fibrinogen gamma chain, N-acetylmuramoyl-L-alanine amidase, immunoglobulin lambda variable 3-21, histone H1.4, attached G-protein coupled receptor G6, immunoglobulin lambda variable 3-25, immunity Globulin lambda variable 1-51, immunoglobulin lambda variable 1-36, mannan-binding lectin serine protease 2, immunoglobulin kappa variable 3-20, immunoglobulin kappa variable 2-30, insulin-like growth factor II, apolipoprotein A-II , probable nonfunctional immunoglobulin kappa variable 2D-24, prothrombin, coagulation factor IX, apolipoprotein L1, 1 protein deleted in malignant brain tumor, desmoglein-3, calcintenin-1, immunoglobulin lambda constant 3, Complement C5, alpha-2-macroglobulin, myosin-9, sodium/potassium transport ATPase subunit gamma, immunoglobulin kappa variable 2-28, oncoprotein-derived transcript 3 protein, serglycin, coagulation factor XII, coagulation factor XIII A chain, insulin, histidine rich glycoprotein, immunoglobulin kappa variable 3-11, immunoglobulin kappa variable 1-39, collagen alpha-1(I) chain, inter-alpha-trypsin inhibitor heavy chain H5, potential transforming growth factor beta binding protein 2, integrin alpha-IIb, membrane-associated progesterone receptor component 1, immunoglobulin lambda variable 6-57, immunoglobulin kappa variable 3-15, complement C1r subcomponent-like protein, histone H1.2, Rho GDP-dissociation inhibitor 2, potential transforming growth factor beta binding protein 4, collagen alpha-1 (XVIII) chain, immunoglobulin lambda variable 2-18, zinc-alpha-2-glycoprotein, talin-1, secretogranin-1, neutrophil defensin 3, Cytochrome P450 2E1, Gastric Inhibitory Polypeptide, Immunoglobulin Heavy Chain Variable 3-15, Immunoglobulin Lambda Variable 2-11, Transcription Initiation Factor TFIID Subunit 1, Collagen Alpha-1 (VII) Chain, Integral Membrane Protein 2B, Pigmented Epithelial Derived Factor , voltage-dependent N-type calcium channel subunit alpha-1B, immunoglobulin lambda variable 3-27, ras GTPase-activating protein nGAP, keratin, type I cytoskeleton 17, tubulin beta chain, sulfhydryl oxidase 1, immunoglobulin Kappa variable 4-1, complement C1r subcomponent, homeobox protein Hox-B2, transcription factor SOX-10, E3 ubiquitin-protein ligase SIAH2, decorin, SPARC, type I collagen alpha-1 chain, type IV collagen alpha -1 chain, laminin gamma 1 chain, vimentin, type III collagen, type IV collagen alpha-3 chain, type VII collagen alpha-1 chain, type VI collagen alpha-1 chain, type V collagen alpha-1 chain, nidogen -1 and type VI collagen alpha-3 chains. 79. The method of any one of claims 76-78, wherein the reporter polypeptide comprises a sequence set forth in columns II-VI of Table A. 80. The method of any one of claims 73-79, wherein the target tissue or cell is characterized by an increased amount or activity of the mammalian protease proximal to the target tissue or cell compared to a non-target tissue or cell of the subject. How to do it. 81. The method of any one of claims 40 to 80, wherein the subject is characterized by increased expression or activity of the mammalian protease proximal to a target tissue or cell compared to a corresponding non-target tissue or cell of the subject. Suffering from or suspected of suffering from a disease or condition. 82. The method of claim 81, wherein the disease or condition is cancer or an inflammatory or autoimmune disease. 83. The method of claim 82, wherein the disease or condition is ankylosing spondylitis (AS), arthritis (eg, rheumatoid arthritis (RA), juvenile idiopathic arthritis (JIA), osteoarthritis (OA), psoriatic arthritis (PsA), gout, chronic arthritis, but not limited to), Chagas disease, chronic obstructive pulmonary disease (COPD), dermatomyositis, type 1 diabetes, endometriosis, Goodpasture syndrome, Graves disease, Guillain-Barré syndrome (GBS), Hashimoto disease , purulent scab, Kawasaki disease, IgA nephropathy, idiopathic thrombocytopenic purpura, inflammatory bowel disease (IBD) (eg, Crohn's disease (CD), clonal disease, ulcerative colitis, collagenous colitis, lymphocytic colitis, ischemic colitis, empty colitis, Behcet's syndrome, infectious colitis, indeterminate colitis, interstitial cystitis, but not limited to), lupus (eg, systemic lupus erythematosus, discoid lupus, subacute cutaneous lupus erythematosus, cutaneous erythematosus lupus (e.g., alumni lupus erythematosus), drug-induced lupus, neonatal lupus, lupus nephritis, but not limited to, mixed connective tissue disease, focal dermatosclerosis, multiple sclerosis (MS), severe muscle weakness, narcolepsy, neuromuscular Angina pectoris, pemphigus vulgaris, pernicious anemia, psoriasis, psoriatic arthritis, polymyositis, primary biliary cirrhosis, recurrent polychondritis, schizophrenia, scleroderma, Sjogren's syndrome, systemic stiffness syndrome, temporal arteritis (also called giant cell arteritis) , vasculitis, vitiligo, Wegener's granulomatosis, immune response associated with transplant rejection (eg, but not limited to, kidney transplant rejection, lung transplant rejection, liver transplant rejection), psoriasis, Wiskott-Aldrich syndrome, autoimmune lymphoproliferative syndrome, myasthenia gravis, chronic inflammatory rhinosinusitis, colitis, chronic digestive disorder, Barrett's esophagus, inflammatory gastritis, autoimmune nephritis, autoimmune hepatitis, autoimmune carditis, autoimmune encephalitis, autoimmune mediated blood disorders, asthma, atopy It is selected from the group consisting of dermatitis, atopy, allergy, allergic rhinitis, scleroderma, bronchitis, and pericarditis, and the inflammatory disease is Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis, inflammatory lung disease, inflammatory skin disease, atherosclerosis, myocardial infarction, stroke, gram-positive shock, gram-negative shock, sepsis, septic shock, hemorrhagic shock, anaphylactic shock, systemic inflammatory response syndrome. 84. The method of claim 83, wherein the disease or condition is carcinoma, Hodgkin's lymphoma and non-Hodgkin's lymphoma, diffuse large B cell lymphoma, follicular lymphoma, mantle cell lymphoma, blastoma, breast cancer, ER/PR+ breast cancer, Her2+ breast cancer, triple negative breast cancer. , colorectal cancer, colorectal cancer with malignant ascites, mucinous tumor, prostate cancer, head and neck cancer, skin cancer, melanoma, genitourinary cancer, ovarian cancer, ovarian cancer with malignant ascites, peritoneal carcinomatosis, uterine serous carcinoma, Endometrial cancer, cervical cancer, colorectal cancer, uterine cancer, peritoneal mesothelioma, kidney cancer, Wilms' tumor, lung cancer, small cell lung cancer, non-small cell lung cancer, gastric cancer, stomach cancer, small intestine cancer, liver cancer, hepatocarcinoma, hepatoblastoma , Liposarcoma, pancreatic cancer, gallbladder cancer, cholangiocarcinoma, esophageal cancer, salivary gland carcinoma, thyroid cancer, epithelial cancer, androgenic germ cell tumor, adenocarcinoma, sarcoma, and B-cell derived chronic lymphocytic leukemia. 85. The method of any one of claims 40-84, wherein the therapeutic agent is an anti-cancer agent. 86. The method of any one of claims 40-85, wherein the therapeutic agent is an activatable therapeutic agent. 87. The method of claim 86, wherein the therapeutic agent is a non-natural, activatable therapeutic agent. 87. The method of any one of claims 40-86, wherein the therapeutic agent comprises a masking moiety (MM). 89. The method of claim 88, wherein the masking moiety (MM) can be released from the therapeutic upon cleavage of the peptide substrate sequence by the mammalian protease. 90. The method of claim 88 or 89, wherein the masking moiety (MM), in its uncleaved state, interferes with the interaction of the therapeutic agent to a target tissue or cell. 91. The method of any one of claims 88-90, wherein the bioactivity of the therapeutic agent can be improved upon cleavage of the peptide substrate sequence by the mammalian protease. 91. The method of any one of claims 88-90, wherein the masking moiety (MM) is an extended recombinant polypeptide (XTEN). 93. The method of claim 92, wherein the XTEN is
(i) contains at least 100 amino acids;
(ii) at least 90% of the amino acid residues are selected from glycine (G), alanine (A), serine (S), threonine (T), glutamate (E) and proline (P);
(iii) at least four different types of amino acids selected from G, A, S, T, E and P. 94. The method of any one of claims 57-93, wherein the subject is determined to be likely to respond to a therapeutic agent. 95. The subject of any one of claims 57 to 94, comprising administering to the subject in need of treatment at least one therapeutically effective dose of an activatable therapeutic agent or a pharmaceutical composition consisting of an activatable therapeutic agent. A method for treating a disease or condition. 96. The method of claim 95, wherein the subject is selected from the group consisting of mouse, rat, monkey and human. 96. The method of claim 95, wherein the subject is a human. 98. The method of any one of claims 95-97, wherein the subject is determined to be likely to respond to the therapeutic agent or the pharmaceutical composition. 99. The method of claim 98, wherein the probability of the reaction is greater than 50%. 101. The method according to claim 99 or 100, wherein said likelihood of said reaction is determined by the method according to any one of claims 1 to 39. 101. The method of any one of claims 95-100, wherein the disease or condition is cancer or an inflammatory or autoimmune disease. 102. The method of claim 101, wherein the disease or condition is ankylosing spondylitis (AS), arthritis (eg, rheumatoid arthritis (RA), juvenile idiopathic arthritis (JIA), osteoarthritis (OA), psoriatic arthritis (PsA), gout, chronic arthritis, but not limited to), Chagas disease, chronic obstructive pulmonary disease (COPD), dermatomyositis, type 1 diabetes, endometriosis, Goodpasture syndrome, Graves disease, Guillain-Barré syndrome (GBS), Hashimoto disease , purulent scab, Kawasaki disease, IgA nephropathy, idiopathic thrombocytopenic purpura, inflammatory bowel disease (IBD) (eg, Crohn's disease (CD), clonal disease, ulcerative colitis, collagenous colitis, lymphocytic colitis, ischemic colitis, empty colitis, Behcet's syndrome, infectious colitis, indeterminate colitis, interstitial cystitis, but not limited to), lupus (eg, systemic lupus erythematosus, discoid lupus, subacute cutaneous lupus erythematosus, cutaneous erythematosus lupus (e.g., alumni lupus erythematosus), drug-induced lupus, neonatal lupus, lupus nephritis, but not limited to, mixed connective tissue disease, focal dermatosclerosis, multiple sclerosis (MS), severe muscle weakness, narcolepsy, neuromuscular Angina pectoris, pemphigus vulgaris, pernicious anemia, psoriasis, psoriatic arthritis, polymyositis, primary biliary cirrhosis, recurrent polychondritis, schizophrenia, scleroderma, Sjogren's syndrome, systemic stiffness syndrome, temporal arteritis (also called giant cell arteritis) , vasculitis, vitiligo, Wegener's granulomatosis, immune response associated with transplant rejection (eg, but not limited to, kidney transplant rejection, lung transplant rejection, liver transplant rejection), psoriasis, Wiskott-Aldrich syndrome, autoimmune lymphoproliferative syndrome, myasthenia gravis, chronic inflammatory rhinosinusitis, colitis, chronic digestive disorder, Barrett's esophagus, inflammatory gastritis, autoimmune nephritis, autoimmune hepatitis, autoimmune carditis, autoimmune encephalitis, autoimmune mediated blood disorders, asthma, atopy It is selected from the group consisting of dermatitis, atopy, allergy, allergic rhinitis, scleroderma, bronchitis, and pericarditis, and the inflammatory disease is Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis, inflammatory lung disease, inflammatory skin disease, atherosclerosis, myocardial infarction, stroke, gram-positive shock, gram-negative shock, sepsis, septic shock, hemorrhagic shock, anaphylactic shock, systemic inflammatory response syndrome. 102. The method of claim 101, wherein the disease or condition is carcinoma, Hodgkin's lymphoma and non-Hodgkin's lymphoma, diffuse large B cell lymphoma, follicular lymphoma, mantle cell lymphoma, blastoma, breast cancer, ER/PR+ breast cancer, Her2+ breast cancer, triple negative breast cancer. , colorectal cancer, colorectal cancer with malignant ascites, mucinous tumor, prostate cancer, head and neck cancer, skin cancer, melanoma, genitourinary cancer, ovarian cancer, ovarian cancer with malignant ascites, peritoneal carcinomatosis, uterine serous carcinoma, Endometrial cancer, cervical cancer, colorectal cancer, uterine cancer, peritoneal mesothelioma, kidney cancer, Wilms' tumor, lung cancer, small cell lung cancer, non-small cell lung cancer, gastric cancer, stomach cancer, small intestine cancer, liver cancer, hepatocarcinoma, hepatoblastoma , Liposarcoma, pancreatic cancer, gallbladder cancer, cholangiocarcinoma, esophageal cancer, salivary gland carcinoma, thyroid cancer, epithelial cancer, androgenic germ cell tumor, adenocarcinoma, sarcoma, and B-cell derived chronic lymphocytic leukemia. Use of a diagnostic reagent in the practice of the method of any one of claims 1 to 39 for assessing the likelihood that a subject suffering from a disease or disorder will respond to a therapeutic agent that can be activated by a mammalian protease expressed in the subject. Usage. Use of a diagnostic reagent in the practice of the method of any one of claims 40 to 103 for assessing the likelihood that a subject suffering from a disease or disorder will respond to a therapeutic agent that can be activated by a mammalian protease expressed in the subject. Usage. To a therapeutic agent capable of being activated by a mammalian protease expressed in a subject suffering from a disease or disorder, including reagents for detecting the presence or amount of proteolytic peptide products produced by the action of the mammalian protease A kit for practicing the method of claims 1 to 103 for assessing the likelihood of reacting.

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